|
Name |
Accession |
Description |
Interval |
E-value |
| RUN_FYCO1 |
cd17698 |
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
7-131 |
6.64e-81 |
|
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and Phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. This model represents the RUN domain of FYCO1.
Pssm-ID: 439060 Cd Length: 158 Bit Score: 262.71 E-value: 6.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 7 ESQLQRIIRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGAND 86
Cdd:cd17698 1 ESQLQKIIRDLQDCVTELKKEFEETGEPITDDSTTLHKFCAKLEYLLQFDQKEKTTLLGGRKDYWDYFCECLAKVKGLND 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1896085763 87 GIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVT 131
Cdd:cd17698 81 GIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVT 125
|
|
| RUN_RUFY4 |
cd17697 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ... |
15-132 |
2.25e-43 |
|
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain; this model represents the RUN domain of RUFY4.
Pssm-ID: 439059 Cd Length: 150 Bit Score: 154.95 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 15 RDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSI 94
Cdd:cd17697 1 KDLQASIAELQKDQEEQQLPITDGSPELHRLCARLEYLLQFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNST 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1896085763 95 SELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTR 132
Cdd:cd17697 81 DKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTG 118
|
|
| RUN_RUFY4_like |
cd17682 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ... |
16-131 |
6.70e-40 |
|
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439044 Cd Length: 150 Bit Score: 145.06 E-value: 6.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 16 DLQDAVTELSKEFqeaGEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKV----KGANDGIRFV 91
Cdd:cd17682 1 DLKGCVLDLKSEF---GEITDPDNPYLRPFCETLEKILRKGLKEKVSLGGRRKDYWDWLEELLKKLnkipKSLSDAVKFV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1896085763 92 KSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVT 131
Cdd:cd17682 78 KSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKLL 117
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1122-1179 |
1.32e-36 |
|
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.
Pssm-ID: 277265 [Multi-domain] Cd Length: 58 Bit Score: 132.30 E-value: 1.32e-36
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1179
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-1002 |
1.30e-28 |
|
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: 125.17 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 195 EVREKQLR---ERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCL 271
Cdd:TIGR02168 221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 272 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQE 351
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 352 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQ-LKEDARASLERLVK-EMAPLQEELSGKGQEADQLWRRLQELL 429
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 430 AHTSSweeeLAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLER-- 507
Cdd:TIGR02168 461 EALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGye 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 508 ----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQE--EELRQANRELEK 575
Cdd:TIGR02168 537 aaieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 576 ELQNVVGRNQLLEGKLQALQadyqalQQRESAIQGSLASLEAEQASIRHL----GDQMEASLLA-------VRKAKEAMK 644
Cdd:TIGR02168 617 ALSYLLGGVLVVDDLDNALE------LAKKLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILErrreieeLEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 645 AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLA 724
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------SKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 725 LSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnrahvQELLQCSERE 804
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL------------RERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 805 GALQEERADEAQQREEELRALQEELSqakcsseeaqLEHAELQEQLhrantdtAELGIQVCALTVEKERVEEALAcavqE 884
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELI-------EELESELEALLNERASLEEALA----L 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 885 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM 964
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQ----------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
810 820 830
....*....|....*....|....*....|....*...
gi 1896085763 965 DYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1002
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
|
| FYVE |
pfam01363 |
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ... |
1121-1184 |
4.09e-25 |
|
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.
Pssm-ID: 426221 [Multi-domain] Cd Length: 68 Bit Score: 99.76 E-value: 4.09e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 1121 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL---SKHGGKKERCCRACFQKLSE 1184
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISllpELGSNKPVRVCDACYDTLQK 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
354-1096 |
1.43e-24 |
|
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: 112.07 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 354 ELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEdarasLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTS 433
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 434 SWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPG 513
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 514 PELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQ------EAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQ-L 586
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 587 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLRE 666
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 667 EVEQCQQLA----------EARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELA---------AQLALSQ 727
Cdd:TIGR02168 511 LLKNQSGLSgilgvlseliSVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsikgTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 728 AQLEVHQGEVQRLQAQVVDLQAKMRAALDD-------QDKVQSQLSMAEAvLREHKTLV---------------QQLKEQ 785
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKK-LRPGYRIVtldgdlvrpggvitgGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 786 NEALNRAhvQELLQCsEREGALQEERADEAQQR----EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 861
Cdd:TIGR02168 670 SSILERR--REIEEL-EEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 862 IQVCALTVEKERVE---EALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 938
Cdd:TIGR02168 747 ERIAQLSKELTELEaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 939 QRAQSLQEAAHQELNTLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCT 1015
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1016 SNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnrERNDQKMLADLDDLNRTKKYLEERLIE 1095
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 1896085763 1096 L 1096
Cdd:TIGR02168 984 L 984
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1121-1183 |
2.23e-24 |
|
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.
Pssm-ID: 214499 [Multi-domain] Cd Length: 68 Bit Score: 97.50 E-value: 2.23e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1121 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLS 1183
Cdd:smart00064 3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGieRPVRVCDDCYENLN 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
541-1051 |
8.20e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 8.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 541 EEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA 620
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 621 SIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV-EQCQQLAEARHRELRALESQCQQQTQLIEVL 699
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 700 TAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAqvvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLV 779
Cdd:COG1196 407 EAEEALL------ERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 780 QQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ-AKCSSEEAQLEHAELQEQLHRANTDTA 858
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVlIGVEAAYEAALEAALAAALQNIVVEDD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 859 ELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 938
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 939 QRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEcKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1018
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
490 500 510
....*....|....*....|....*....|...
gi 1896085763 1019 LAECQAAMLRKDKEGAALREDLERTQKELEKAT 1051
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-915 |
9.41e-21 |
|
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: 99.75 E-value: 9.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 178 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaedNVRLTCLVAELQKQWEVT 257
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 258 QATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 337
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 338 KGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE---------QLVKELQLKEDARASLERLVKEMAPLQ 408
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 409 EELSGKGQEADQLWRRLQEL---LAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQF-------LETQLAQVS 478
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVdegyeaaIEAALGGRL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 479 QH--VSDLEEQKKQLIQDKDHLSQQVGML---------------ERLAGPPG------------PELPVAGEKNEALVPV 529
Cdd:TIGR02168 548 QAvvVENLNAAKKAIAFLKQNELGRVTFLpldsikgteiqgndrEILKNIEGflgvakdlvkfdPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 530 NSSLQEAWGKPEEEQRGLQEAQLDDTKV-----------------QEGSQE--------EELRQANRELEKELQNVVGRN 584
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssiLERRREieeleekiEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 585 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 664
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 665 REEVEQCQQLAEARHRELRALESQCQQQTqlIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQV 744
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 745 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRaHVQELlqcserEGALQEERADEAQQREEELRA 824
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-KRSEL------RRELEELREKLAQLELRLEGL 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 825 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEaasrEREGLERQVA 904
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE----RYDFLTAQKE 1010
|
810
....*....|.
gi 1896085763 905 GLQQEKESLQE 915
Cdd:TIGR02168 1011 DLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-1054 |
3.75e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 352 MQELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARaslerlvkemapLQEELSGKGQEADQLWRRLQELLAH 431
Cdd:COG1196 195 LGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRE------------LEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 432 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmlerlagp 511
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 512 pgpelpvAGEKNEALVPVNSSLQEAwgkpeEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQnvvgRNQLLEGKL 591
Cdd:COG1196 332 -------LEELEEELEELEEELEEA-----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----ELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 592 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 671
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 672 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 751
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 752 RAALDDQDKVQSQlsmAEAVLREHKtlvqQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 831
Cdd:COG1196 549 QNIVVEDDEVAAA---AIEYLKAAK----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 832 AkcssEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcAVQELQDAKEAASREREGLERQVAGLQQEKE 911
Cdd:COG1196 622 L----LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG-SRRELLAALLEAEAELEELAERLAEEELELE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 912 SLQEKLKAAKAAagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEckslrgqlEEQGRQL 991
Cdd:COG1196 697 EALLAEEEEERE------LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE--------LPEPPDL 762
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 992 QAAEEAVEKLKATQADMGeklscTSNHLAECQAAMLRKDKEG-AALREDLERTQKELEKATTKI 1054
Cdd:COG1196 763 EELERELERLEREIEALG-----PVNLLAIEEYEELEERYDFlSEQREDLEEARETLEEAIEEI 821
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-813 |
2.86e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 199 KQLRERMQQLDREnqELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGA 278
Cdd:COG1196 216 RELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 279 AEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASfpgwlamAQQKADTASDtkgrqepipsDAAQEMQELGEK 358
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-------LEEELEELEE----------ELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 359 LQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEE 438
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 439 LAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAGPPGPELPV 518
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 519 AGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQEEELRQ---------ANRELEKELQNVVGR 583
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 584 NQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQ 663
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 664 LREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQ 743
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEER-----------------ELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 744 VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHktlVQQLKEQNEAL---NRAHVQELLQCSEREGALQEERAD 813
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERE---LERLEREIEALgpvNLLAIEEYEELEERYDFLSEQRED 806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
772-1118 |
5.16e-18 |
|
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: 90.50 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 772 LREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLH 851
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 852 RANTDTAELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQ 931
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 932 AQLAQAEQRAQSLQEAAHQELNTLKfqlsaeimdyqSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1011
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLR-----------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1012 LS-----CTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTK 1086
Cdd:TIGR02168 430 LEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-AQLQARLDSLERLQENLEGFSEGV 508
|
330 340 350
....*....|....*....|....*....|..
gi 1896085763 1087 KYLEERLIELLRDKDALWqksDALEFQQKLSA 1118
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLS---ELISVDEGYEA 537
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1130-1179 |
6.79e-18 |
|
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.
Pssm-ID: 277249 [Multi-domain] Cd Length: 52 Bit Score: 78.73 E-value: 6.79e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 1130 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1179
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1122-1180 |
2.86e-17 |
|
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.
Pssm-ID: 277264 [Multi-domain] Cd Length: 62 Bit Score: 76.98 E-value: 2.86e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACFQ 1180
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
236-913 |
3.63e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 236 AAEDN-VRLTCLVAELQKQWEV--TQATQ-NTVKELQTCLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSL 310
Cdd:COG1196 183 ATEENlERLEDILGELERQLEPleRQAEKaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 311 DKKNQHLASfpgwLAMAQQKADTASDTKGrqepipsdaaQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL- 389
Cdd:COG1196 263 AELEAELEE----LRLELEELELELEEAQ----------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 390 ---KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekelleqevrSLTRQ 466
Cdd:COG1196 329 eeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---------------------ELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 467 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvageknealvpvnsslqeawgkpEEEQRG 546
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERL------------------------------------------EEELEE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 547 LQEAQLddtkvQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 626
Cdd:COG1196 426 LEEALA-----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 627 DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALEsqcqqqtQLIEVLTAEKGQQ 706
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA-------AAIEYLKAAKAGR 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 707 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 786
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 787 EALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKcSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 866
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-AEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1896085763 867 LTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESL 913
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1121-1179 |
4.46e-17 |
|
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.
Pssm-ID: 277269 [Multi-domain] Cd Length: 63 Bit Score: 76.67 E-value: 4.46e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1896085763 1121 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1179
Cdd:cd15730 2 KWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACF 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
641-1013 |
4.64e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 641 EAMKAQMAEKEAILQSKEGECQQLREEVEQcqqlAEaRHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdnEARELA 720
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEK----AE-RYRELKEELKELEAELLLLKLRELEA-----------ELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 721 AQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAHVQEllqc 800
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 801 sEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvEKERVEEALAC 880
Cdd:COG1196 319 -EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 881 AVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLS 960
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE----------LEEALAELEEEEEEEEEALEEAAEEEA-ELE 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 961 AEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLS 1013
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
773-1092 |
1.22e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 773 REHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHR 852
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 853 ANTDTAELgiqvcaltvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQA 932
Cdd:COG1196 293 LLAELARL-----------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 933 QLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1012
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1013 SCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTKKYLEER 1092
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
351-1093 |
1.11e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 351 EMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGkgQEADQLWRRLQELLA 430
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE--EEQLRVKEKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 431 HTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAG 510
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 511 PPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTkvqegSQEEELRQANRELEKELQNVVGRNQLLEGK 590
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN-----AAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 591 LQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGecqqlreeveQ 670
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG----------T 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 671 CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGV--------GPPTDNEARELAAQLALSQAqleVHQGEVQRLQA 742
Cdd:TIGR02169 527 VAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIellkrrkaGRATFLPLNKMRDERRDLSI---LSEDGVIGFAV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 743 QVVDLQAKMRAA----LDDQDKVQSqLSMAEAVLREHK--TLVQQLKEQNEALNRAHVQ-------------ELLQCSER 803
Cdd:TIGR02169 604 DLVEFDPKYEPAfkyvFGDTLVVED-IEAARRLMGKYRmvTLEGELFEKSGAMTGGSRAprggilfsrsepaELQRLRER 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 804 EGALQEERADEAQQREE---ELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAC 880
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 881 AVQELQDAKEAASREREGLERQVAGLQQEK-ESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfql 959
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ--- 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 960 sAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQaamlRKDKEGAALRED 1039
Cdd:TIGR02169 840 -EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE----RKIEELEAQIEK 914
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 1040 LERTQKELeKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 1093
Cdd:TIGR02169 915 KRKRLSEL-KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1121-1179 |
1.56e-15 |
|
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.
Pssm-ID: 277270 [Multi-domain] Cd Length: 65 Bit Score: 72.38 E-value: 1.56e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 1121 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACF 1179
Cdd:cd15731 4 LWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCsSNSVPLPRYGqMKPVRVCNHCF 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
548-1103 |
1.86e-15 |
|
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: 82.41 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 548 QEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 624
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 625 LGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHR------------------------ 680
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqletlrskvaqlelqia 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 681 ----ELRALESQCQQQTQLIEVLTAEKGQQGvGPPTDNEARELAAQLALS-------QAQLEVHQGEVQRLQAQVVDLQA 749
Cdd:TIGR02168 397 slnnEIERLEARLERLEDRRERLQQEIEELL-KKLEEAELKELQAELEELeeeleelQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 750 KMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAH-----VQELLQCSER-----EGALQE---------- 809
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvLSELISVDEGyeaaiEAALGGrlqavvvenl 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 810 ---ERADEAQQREEELRALQEELSQAK------------------------CSSEEAQLEHA------------ELQEQL 850
Cdd:TIGR02168 556 naaKKAIAFLKQNELGRVTFLPLDSIKgteiqgndreilkniegflgvakdLVKFDPKLRKAlsyllggvlvvdDLDNAL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 851 HRANTDTAELGI-------------------QVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 911
Cdd:TIGR02168 636 ELAKKLRPGYRIvtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 912 SLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGE---ECKSLRGQLEEQ- 987
Cdd:TIGR02168 716 QLRKELEELSRQ---ISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELEERLEEAEEelaEAEAEIEELEAQi 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 988 ----------GRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT---KI 1054
Cdd:TIGR02168 792 eqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieEL 871
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1896085763 1055 QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL 1103
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
345-1075 |
5.28e-15 |
|
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: 80.78 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 345 PSDAAQEMQELgEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKED--------ARASLERLVKEMAPLQEELSGKGQ 416
Cdd:TIGR00618 162 SKEKKELLMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpdtYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 417 EADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLetQLAQVSQHVSDLEEQKKQLIQDkd 496
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTE-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 497 hLSQQVGMLERLAGPPGPELpvageKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLD--DTKVQEGSQEEELRQANRELE 574
Cdd:TIGR00618 316 -LQSKMRSRAKLLMKRAAHV-----KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 575 KELQNVVGRNQLLEgKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASL---LAVRKAKEAMKAQMAEKE 651
Cdd:TIGR00618 390 TLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAItctAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 652 AILQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEvLTAEKGQQGVGPPTDNEARELAAQLALSQAQLE 731
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLELQ--EEPCPLCGSCIH-PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 732 VHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 811
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 812 ADeaQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAntdtaelgiqvcALTVEKERVEEALACAVQELQDAKEA 891
Cdd:TIGR00618 626 DL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL------------SIRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 892 ASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQ-RAQSLQEAAHQELNTLKFQLSAEIMDYQSRL 970
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDaLNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 971 --KNAGEECKSLRGQLEEQGRQLqaaEEAVEKLKATQADMGEKLsctsnhlaecQAAMLRKDKEGAALREDLERTQKELE 1048
Cdd:TIGR00618 772 aaLQTGAELSHLAAEIQFFNRLR---EEDTHLLKTLEAEIGQEI----------PSDEDILNLQCETLVQEEEQFLSRLE 838
|
730 740
....*....|....*....|....*..
gi 1896085763 1049 KATTKIQEYYNKLCQEVTNRERNDQKM 1075
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLT 865
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1122-1182 |
1.06e-14 |
|
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.
Pssm-ID: 277268 [Multi-domain] Cd Length: 68 Bit Score: 70.07 E-value: 1.06e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1182
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSlKARLEYLDNKEARVCVPCYQTL 68
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-976 |
1.75e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 519 AGEKNEALVPV---NSSLQEAWgkpeeEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQNVVGRNQLLEGKLQAL 594
Cdd:COG4913 247 AREQIELLEPIrelAERYAAAR-----ERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 595 QADYQALQQRESAIQGS-LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQ 673
Cdd:COG4913 322 REELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 674 LAEARHRELRALESQCQQQ-TQLIEVLTAEKGQQGVGPPTDNEAR-ELAAQLALSQAQL-------EVHQGEV------- 737
Cdd:COG4913 402 ALEEALAEAEAALRDLRRElRELEAEIASLERRKSNIPARLLALRdALAEALGLDEAELpfvgeliEVRPEEErwrgaie 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 738 -------------QRLQAQVVDL--QAKMRAALDDQdKVQSQLSMAEAVLREHKTLVQQLK-EQNEAlnRAHVQELLQ-- 799
Cdd:COG4913 482 rvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYE-RVRTGLPDPERPRLDPDSLAGKLDfKPHPF--RAWLEAELGrr 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 800 ----CSEREGALQEER----------------------------------ADEAQQREEELRALQEELSQAKCSSEEAQL 841
Cdd:COG4913 559 fdyvCVDSPEELRRHPraitragqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 842 EHAELQEQLHRANT---------DTAELGIQVCALTVEKERVE------EALACAVQELQDAKEAASREREGLERQVAGL 906
Cdd:COG4913 639 ELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRL 718
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 907 QQEKESLQEKLKAAKAAAGSLPGLQAQLAQA---EQRAQSLQEAAHQElntLKFQLSAEIMDYQSRLKNAGEE 976
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERE---LRENLEERIDALRARLNRAEEE 788
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1122-1179 |
4.26e-14 |
|
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277261 [Multi-domain] Cd Length: 58 Bit Score: 68.18 E-value: 4.26e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1179
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1121-1179 |
4.58e-14 |
|
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.
Pssm-ID: 277271 [Multi-domain] Cd Length: 61 Bit Score: 68.00 E-value: 4.58e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 1121 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACF 1179
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQklPVPSQQLFEPSRVCKSCF 61
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
179-731 |
1.00e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 179 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQ 258
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 259 ATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFpgwLAMAQQKADTASDTK 338
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 339 GRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEA 418
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 419 DQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTrqlqfLETQLAQVSQH-VSDLEEQKKQLIQDkdh 497
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-----LEAALAAALQNiVVEDDEVAAAAIEY--- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 498 lsqqvgmLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRElekel 577
Cdd:COG1196 566 -------LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE----- 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 578 qNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgdQMEASLLAVRKAKEAMKAQMAEKEAILQSK 657
Cdd:COG1196 634 -AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE--LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 658 EGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqgvgPPTDNEARELAAQLALSQAQLE 731
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE-------LPEPPDLEELERELERLEREIE 777
|
|
| RUN |
cd17671 |
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ... |
14-133 |
1.40e-13 |
|
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.
Pssm-ID: 439038 Cd Length: 154 Bit Score: 69.76 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 14 IRDLQDAVTELSKEFQEAGEPITDDSTSLHKFSYKLEYLLQFDQKEKAtLLGNKKDYWDYFCACLAKVKGANDG--IRFV 91
Cdd:cd17671 3 VKELLESFADNGEADDSAALTLTDDDPVVGRLCAALEAILSHGLKPKR-FGGGKVSFWDFLEALEKLLPAPSLKqaIRDI 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1896085763 92 KSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTRR 133
Cdd:cd17671 82 NSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRK 123
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1122-1179 |
1.47e-13 |
|
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.
Pssm-ID: 277272 [Multi-domain] Cd Length: 60 Bit Score: 66.69 E-value: 1.47e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1122 WLGDTEANHCLDCKREFsWMV-RRHHCRICGRIFCYYCCNnyvlSKHGGKKE------RCCRACF 1179
Cdd:cd15733 1 WVPDHAASHCFGCDCEF-WLAkRKHHCRNCGNVFCADCSN----YKLPIPDEqlydpvRVCNSCY 60
|
|
| FYVE_ZF21 |
cd15727 |
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ... |
1119-1164 |
1.53e-13 |
|
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.
Pssm-ID: 277266 [Multi-domain] Cd Length: 64 Bit Score: 66.63 E-value: 1.53e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1896085763 1119 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL 1164
Cdd:cd15727 1 EPPWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVP 46
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
180-1097 |
1.81e-13 |
|
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: 75.87 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 180 ALEGFDEMRLELDQLEVREKQLRERMQQLdrenqelraavsqQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA 259
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERL-------------RREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 260 TQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKnqhLASFPGWLAMAQQKADtasdtkg 339
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIA------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 340 rqepipsDAAQEMQELGEKLQALERERTKVEEvnrqqsaQLEQLVKELqlkedaraslERLVKEMAPLQEELSGKGQEAD 419
Cdd:TIGR02169 312 -------EKERELEDAEERLAKLEAEIDKLLA-------EIEELEREI----------EEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 420 QLWRRLQELLAHTSSWEeelaelrREKKQQQEEKELLEQEVRSLTRQ-------LQFLETQLAQVSQHVSDLEEQKKQLI 492
Cdd:TIGR02169 368 DLRAELEEVDKEFAETR-------DELKDYREKLEKLKREINELKREldrlqeeLQRLSEELADLNAAIAGIEAKINELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 493 QDKDHLSQQVGMLERlagppgpELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE--AQLDDTKVQEGSQEEELRQAN 570
Cdd:TIGR02169 441 EEKEDKALEIKKQEW-------KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelAEAEAQARASEERVRGGRAVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 571 RELEKELQNVVGrnqlLEGKLQALQADYQAlqQRESAIQGSLASLEAE-----QASIRHLGDQM--EASLLAVRKakeaM 643
Cdd:TIGR02169 514 EVLKASIQGVHG----TVAQLGSVGERYAT--AIEVAAGNRLNNVVVEddavaKEAIELLKRRKagRATFLPLNK----M 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 644 KAQMAEKEAIlqSKEGECQQLREEVEQCQQLAEA------------RHRELRALESQCQQQTQLIEVL----------TA 701
Cdd:TIGR02169 584 RDERRDLSIL--SEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvveDIEAARRLMGKYRMVTLEGELFeksgamtggsRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 702 EKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQ 781
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 782 LKEQnealnRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAELQeqlhrantdtaELG 861
Cdd:TIGR02169 739 LEEL-----EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----NDLEARLSHSRIP-----------EIQ 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 862 IQVCALTVEKERVEEALACAVQELQD---AKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAE 938
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 939 QRAQSLQeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1018
Cdd:TIGR02169 868 EELEELE---------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1019 LAECQAAmLRKDKEGAALREDLERTQKELEKATTKIQEYynklcQEVTNRERND-QKMLADLDDLNRTKKYLEERLIELL 1097
Cdd:TIGR02169 933 LSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIRAL-----EPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1127-1179 |
7.80e-13 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.
Pssm-ID: 277299 [Multi-domain] Cd Length: 59 Bit Score: 64.63 E-value: 7.80e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 1127 EANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHGGKKERC--CRACF 1179
Cdd:cd15760 4 PDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIpLPHLGPLGVPQrvCDRCF 59
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1122-1178 |
1.47e-12 |
|
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.
Pssm-ID: 277297 [Multi-domain] Cd Length: 71 Bit Score: 64.32 E-value: 1.47e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1178
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSC 62
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-971 |
1.56e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 347 DAAQEMQELgekLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQeelsgkgqeadqLWRRLQ 426
Cdd:COG4913 225 EAADALVEH---FDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAALR------------LWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 427 ELLAhtssWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVS-QHVSDLEEQKKQLIQDKDHLSQQVGML 505
Cdd:COG4913 289 RLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 506 ERLAGPPGPELPVAGEKNEALVPVNSSLQEAWgkpeEEQRGLQEAQLDDTKVqegsQEEELRQANRELEKELQNVVGRNQ 585
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEAL----EEELEALEEALAEAEA----ALRDLRRELRELEAEIASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 586 LLEGKLQALQADY-QALQQRES--------------------AIQGSLASL------EAEQAS-----IRHLGDQMEASL 633
Cdd:COG4913 437 NIPARLLALRDALaEALGLDEAelpfvgelievrpeeerwrgAIERVLGGFaltllvPPEHYAaalrwVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 634 LAVRKAKEAMKAQMAEKEAI---LQSKEGECQQ-LREEVEQ-----CQQLAEARHRELRALESQCQ--QQTQLievltAE 702
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSLagkLDFKPHPFRAwLEAELGRrfdyvCVDSPEELRRHPRAITRAGQvkGNGTR-----HE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 703 KGQQGVGPPT-----DNEAR--ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmRAALDDQDKVQSQLSMAEAVLREh 775
Cdd:COG4913 592 KDDRRRIRSRyvlgfDNRAKlaALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAERE- 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 776 ktlVQQLKEQNEALNRAHvQELLQCSEREGALQEERaDEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANT 855
Cdd:COG4913 670 ---IAELEAELERLDASS-DDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 856 DTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE-KESLQEKLKAAKAAAGSLPGLQAQL 934
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALL 821
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1896085763 935 AQ--------AEQR-AQSLQEAAHQELNTLKFQLSAEIMDYQSRLK 971
Cdd:COG4913 822 DRleedglpeYEERfKELLNENSIEFVADLLSKLRRAIREIKERID 867
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
813-1120 |
1.75e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 813 DEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEealacaVQELQDAKEAA 892
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE------LEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 893 SREREGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKN 972
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL--------------EELEEELAELEEELEELEEELEELE----EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 973 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1052
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1896085763 1053 KIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1120
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1126-1182 |
1.83e-12 |
|
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.
Pssm-ID: 277260 [Multi-domain] Cd Length: 61 Bit Score: 63.56 E-value: 1.83e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1896085763 1126 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACFQKL 1182
Cdd:cd15720 3 KDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSsTIPKFGIEKEvRVCDPCYEKL 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
463-1119 |
1.92e-12 |
|
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: 72.41 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 463 LTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpelpvagekneaLVPVNSSLQEawgKPEE 542
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL-----------------LEELNKKIKD---LGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 543 EQRGLQEaQLDDTKVQEGSQEEELRQANRELEKelqnvvgrnqlLEGKLQALQADYqalqqreSAIQGSLASLEAEQASI 622
Cdd:TIGR02169 288 EQLRVKE-KIGELEAEIASLERSIAEKERELED-----------AEERLAKLEAEI-------DKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 623 RHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAE 702
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 703 -KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 781
Cdd:TIGR02169 429 iAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 782 LKEQNEALNR------AHVQELLQCSERE---------GALQ------EERADEAQQREEE----------LRALQEELS 830
Cdd:TIGR02169 509 GRAVEEVLKAsiqgvhGTVAQLGSVGERYataievaagNRLNnvvvedDAVAKEAIELLKRrkagratflpLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 831 QAKCSSEEAQLEHA----ELQEQLHRA------------NTDTA-ELGIQVCALTVEKERVE-----------EALACAV 882
Cdd:TIGR02169 589 DLSILSEDGVIGFAvdlvEFDPKYEPAfkyvfgdtlvveDIEAArRLMGKYRMVTLEGELFEksgamtggsraPRGGILF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 883 QELQDAKEAASRER-EGLERQVAGLQQEKESLQ----EKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHqelntlkf 957
Cdd:TIGR02169 669 SRSEPAELQRLRERlEGLKRELSSLQSELRRIEnrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-------- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 958 QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADmgEKLSCTSNHLAECQAAMLRKDKEGAALR 1037
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1038 EDLERTQKELEKATTKIQEYYNKL----------CQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL-WQK 1106
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRidlkeqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeAQL 898
|
730
....*....|...
gi 1896085763 1107 SDALEFQQKLSAE 1119
Cdd:TIGR02169 899 RELERKIEELEAQ 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-1103 |
3.25e-12 |
|
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: 71.64 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 354 ELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL-KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAht 432
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQALLKEKREYEGYELLKeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 433 ssweEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVgmlerlagpp 512
Cdd:TIGR02169 273 ----LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI---------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 513 gpelpvageknealvpvnsslqeawgkpEEEQRGLQEAQLDDTKVQEgsQEEELRQANRELEKELQNVVGRNQLLEGKLQ 592
Cdd:TIGR02169 339 ----------------------------EELEREIEEERKRRDKLTE--EYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 593 ALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQ 672
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 673 QLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARE-----------LAAQL----ALSQAQLEVHQGev 737
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgTVAQLgsvgERYATAIEVAAG-- 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 738 QRLQAQVVDLQA-----------------------KMRAALDDQDK--------------------------------VQ 762
Cdd:TIGR02169 547 NRLNNVVVEDDAvakeaiellkrrkagratflplnKMRDERRDLSIlsedgvigfavdlvefdpkyepafkyvfgdtlVV 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 763 SQLSMAEAVLREHK--TLVQQLKEQNEALNRAHVQ-------------ELLQCSEREGALQEERADEAQqreeELRALQE 827
Cdd:TIGR02169 627 EDIEAARRLMGKYRmvTLEGELFEKSGAMTGGSRAprggilfsrsepaELQRLRERLEGLKRELSSLQS----ELRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 828 ELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgiqvcaltveKERVEEaLACAVQELQDAKEAASREREGLERQVAGLQ 907
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKL----------KERLEE-LEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 908 QEKESLQEKLKAakaaagslpgLQAQLAQaeQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQ 987
Cdd:TIGR02169 772 EDLHKLEEALND----------LEARLSH--SRIPEIQAEL-SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 988 GRQLQAAEEAVEKLKATQADMGEKLsctsnhlaecqAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTN 1067
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKK-----------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820 830
....*....|....*....|....*....|....*.
gi 1896085763 1068 RERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL 1103
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
571-1135 |
4.34e-12 |
|
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: 71.30 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 571 RELEKELQNVVGRNQLLEGKLQALQADYQ-----ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKA 645
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 646 QMAEKEAI----LQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 721
Cdd:pfam15921 307 QARNQNSMymrqLSDLESTVSQLRSELREAKRMYEDKIEELE--KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 722 -------QLALSQAQ---------------------LEVHQGEVQRLQAQVVDLQAKMRAALDDQdkvQSQLSMAEAVLR 773
Cdd:pfam15921 385 dlhkrekELSLEKEQnkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQ---MAAIQGKNESLE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 774 EHKTLVQQLKEQNEALnRAHVQEL------LQCSERE-----GALQE-ERADEAQQRE------------EELRALQEE- 828
Cdd:pfam15921 462 KVSSLTAQLESTKEML-RKVVEELtakkmtLESSERTvsdltASLQEkERAIEATNAEitklrsrvdlklQELQHLKNEg 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 829 --LSQAKCSSEEAQLEHAE-------LQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQ------DAKEAAS 893
Cdd:pfam15921 541 dhLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkDKKDAKI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 894 REregLERQVAGLQQEKESLqeklkaakAAAGSlPGLQAQLAQAEQRAQSLQEA--AHQELNTLkfqlSAEIMDYQSRLK 971
Cdd:pfam15921 621 RE---LEARVSDLELEKVKL--------VNAGS-ERLRAVKDIKQERDQLLNEVktSRNELNSL----SEDYEVLKRNFR 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 972 NAGEECKSLRGQLEeqgRQLQAAEEAVEKLKATQADMgeklSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKAT 1051
Cdd:pfam15921 685 NKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1052 TK-------IQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL--IELLRDKDALwQKSDALEFQQKLSAEERW 1122
Cdd:pfam15921 758 TNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL-QFAECQDIIQRQEQESVR 836
|
650
....*....|...
gi 1896085763 1123 LgdtEANHCLDCK 1135
Cdd:pfam15921 837 L---KLQHTLDVK 846
|
|
| RUN_RUNDC3 |
cd17684 |
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ... |
33-133 |
4.46e-12 |
|
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.
Pssm-ID: 439046 Cd Length: 150 Bit Score: 65.11 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGN--KKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17684 20 ETIDDSSEELINFAAILEQILSHRLKPVKPWYGSeePRTFWDYIRVACKKV--PQNCIASIEQMENIKSPKAKGRAWIRV 97
|
90 100
....*....|....*....|...
gi 1896085763 111 SLVHQRLADTLQQCFMNTKVTRR 133
Cdd:cd17684 98 ALMEKRLSEYLSTALKQTRLTRN 120
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
536-914 |
4.46e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 536 AWGKPEEEQRGLQEAQLddtkvqegSQEEELRQANRELEKE---LQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSL 612
Cdd:PRK04863 273 DYMRHANERRVHLEEAL--------ELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 613 ASLEAE---QASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------L 682
Cdd:PRK04863 345 RQQEKIeryQADLEELEERLEEQNEVVEEADE----QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 683 RALESqCQQQTQL-----------IEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQ 741
Cdd:PRK04863 421 QALER-AKQLCGLpdltadnaedwLEEFQAKEQEA------TEELLSLEQKLSVAQAAHSQFEqayqlvrkiaGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 742 AQVVdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvQELLQCSEREGALQEERADEAQQREEE 821
Cdd:PRK04863 494 AWDV-----ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA------ERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 822 LRALQEELSQAKCSSEEAQLEHAELQEQL--------------HRANTDTAELGIQVCALTVEKERVEEALacavQELQD 887
Cdd:PRK04863 563 LEARLESLSESVSEARERRMALRQQLEQLqariqrlaarapawLAAQDALARLREQSGEEFEDSQDVTEYM----QQLLE 638
|
410 420
....*....|....*....|....*..
gi 1896085763 888 AKEAASREREGLERQVAGLQQEKESLQ 914
Cdd:PRK04863 639 RERELTVERDELAARKQALDEEIERLS 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-832 |
4.58e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 283 EDYHTALRRLE---SMLQPL---AQELEATRDSLDKKNQHLASFPGWlaMAQQKADTASDTKGRQEPIPSDAAQEMQELG 356
Cdd:COG4913 238 ERAHEALEDAReqiELLEPIrelAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 357 EKLQALERERTKVEEVNRQQS--------AQLEQLVKELQLKEDARASLERLVKEmapLQEELSGkgqEADQLWRRLQEL 428
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAA---LGLPLPA---SAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 429 LAHTSSWEEELAELRREkkqqqeekelleqeVRSLTRQLQFLETQLAQVSQHVSDLEEQKK----QLIQDKDHLSQQVGM 504
Cdd:COG4913 390 AALLEALEEELEALEEA--------------LAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 505 LERlagppgpELPVAGEkneaLVPVnsslqeawgKPEEEQ-RGLQEAQLddtkvqeGSQ-------EEELRQANReleke 576
Cdd:COG4913 456 DEA-------ELPFVGE----LIEV---------RPEEERwRGAIERVL-------GGFaltllvpPEHYAAALR----- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 577 lqnVVGRNQLlEGKLQALQAD-YQALQQRESAIQGSLAS-LEAEQASIR-----HLGDQM-------EASLLAVRKA--K 640
Cdd:COG4913 504 ---WVNRLHL-RGRLVYERVRtGLPDPERPRLDPDSLAGkLDFKPHPFRawleaELGRRFdyvcvdsPEELRRHPRAitR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 641 EAM---KAQMAEK----------------EAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTA 701
Cdd:COG4913 580 AGQvkgNGTRHEKddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 702 EKGQQGVgpptDNEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 781
Cdd:COG4913 660 EIDVASA----EREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 782 LKEQNEALNRAHVQELLQCSE--REGALQEERADEAQQR-EEELRALQEELSQA 832
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEerFAAALGDAVERELRENlEERIDALRARLNRA 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
563-947 |
5.30e-12 |
|
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: 70.87 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 563 EEELRQANRELEKELQNVvGRNQLLEG----KLQALQAD------YQALQQRESAIQGSLASLEaeqasirhlgdqmeas 632
Cdd:TIGR02169 169 DRKKEKALEELEEVEENI-ERLDLIIDekrqQLERLRRErekaerYQALLKEKREYEGYELLKE---------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 633 LLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQlievltaekgqqgvgppt 712
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------------------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 713 dNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEqnEALNRA 792
Cdd:TIGR02169 294 -EKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-------EIDKLLAEIEELEREIEEERKRRDKLTE--EYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 793 HVQELLQCSeregaLQEERADEAQQREEeLRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQvcaLTVEKE 872
Cdd:TIGR02169 364 EELEDLRAE-----LEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA---IAGIEA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 873 RVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEA 947
Cdd:TIGR02169 435 KINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE---LSKLQRELAEAEAQARASEER 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
809-1121 |
6.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 809 EERADEAQQREEELRALQEELsqakcsseEAQLEHAELQ-EQLHRANTDTAELGI-QVCALTVEKERVEEALACAVQELQ 886
Cdd:COG1196 178 ERKLEATEENLERLEDILGEL--------ERQLEPLERQaEKAERYRELKEELKElEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 887 DAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDY 966
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 967 QSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKE 1046
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1047 LEKATTKIQEYYnklcQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1121
Cdd:COG1196 409 EEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1119-1179 |
6.61e-12 |
|
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.
Pssm-ID: 277278 [Multi-domain] Cd Length: 73 Bit Score: 62.36 E-value: 6.61e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 1119 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1179
Cdd:cd15739 1 EVRWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1130-1179 |
7.74e-12 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.
Pssm-ID: 277284 [Multi-domain] Cd Length: 52 Bit Score: 61.36 E-value: 7.74e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 1130 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1179
Cdd:cd15745 1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVpdTCIYLRVCKTCY 52
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
1122-1179 |
9.85e-12 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277257 [Multi-domain] Cd Length: 61 Bit Score: 61.23 E-value: 9.85e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1122 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE-RCCRACF 1179
Cdd:cd15717 2 WVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHQSSKPlRVCDTCY 61
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
171-1048 |
1.00e-11 |
|
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: 70.15 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 171 DLNSPLNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQT---ERERGRTAAEDNVRltclv 247
Cdd:pfam15921 60 ELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTklqEMQMERDAMADIRR----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 248 AELQKQWEVTQATQNTVKELQT--CLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSLDKK--------NQH 316
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAakCLKEDMLEDSNTQiEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmsTMH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 317 LASFPGWLAMAQQKADTA-SDTKGRQEPIPsdaaqemqelgEKLQALERE-RTKVEEVNRQQSAQLEQLVKELQLK---- 390
Cdd:pfam15921 215 FRSLGSAISKILRELDTEiSYLKGRIFPVE-----------DQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEitgl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 391 ----EDARASLERLVKEMAPLQEElsGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSltrQ 466
Cdd:pfam15921 284 tekaSSARSQANSIQSQLEIIQEQ--ARNQNSMYM-RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS---E 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 467 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgmlerlagppgpELPVAGEKNEALvpvnsslqeaWgkpeeeqrg 546
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREK--------------ELSLEKEQNKRL----------W--------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 547 lqeaqldDTKVQEGSQEEELRqanRELEKELQNVvgrnQLLEGKLQALQADYQA-LQQRESAIQGSLASLEaeqaSIRHL 625
Cdd:pfam15921 405 -------DRDTGNSITIDHLR---RELDDRNMEV----QRLEALLKAMKSECQGqMERQMAAIQGKNESLE----KVSSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 626 GDQMEASLLAVRKAKEAMKAqmaeKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkGQ 705
Cdd:pfam15921 467 TAQLESTKEMLRKVVEELTA----KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 706 QGVGPPTDNEARELaaQLALSQAQLEVHQGEVQRLqAQVVDLQAKMRAALD-DQDKVQSQLSMAEAVLREHKTL------ 778
Cdd:pfam15921 542 HLRNVQTECEALKL--QMAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQEFKILkdkkda 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 779 -VQQLKEQNEALNRAHVQELLQCSEREGALQeeraDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT 857
Cdd:pfam15921 619 kIRELEARVSDLELEKVKLVNAGSERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 858 AELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQA 937
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF----------LEEAMTNA 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 938 EQRAQSLQEAahqelntlKFQLSAEimdyqsrLKNAGEECKSLRGQLEeqgrQLQAAEeavEKLKATQADMGEKLSCTSN 1017
Cdd:pfam15921 761 NKEKHFLKEE--------KNKLSQE-------LSTVATEKNKMAGELE----VLRSQE---RRLKEKVANMEVALDKASL 818
|
890 900 910
....*....|....*....|....*....|.
gi 1896085763 1018 HLAECQAAMLRKDKEGAALREDLERTQKELE 1048
Cdd:pfam15921 819 QFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| RUN_RUFY1_like |
cd17681 |
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ... |
20-133 |
2.26e-11 |
|
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439043 Cd Length: 155 Bit Score: 63.36 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 20 AVTELS-KEFQEA----GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSI 94
Cdd:cd17681 7 NLAKLSiKELIESalsfGRTLDSDHVPLQQFFVILEHVLRHGLKVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVRDL 86
|
90 100 110
....*....|....*....|....*....|....*....
gi 1896085763 95 SELRTSLGKGRAFIRYSLVHQRLADTLqQCFMNTKVTRR 133
Cdd:cd17681 87 PGIKTPLGRARAWLRLALMQKKLADYF-RALIENKDLLS 124
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
186-986 |
2.70e-11 |
|
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: 68.83 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 186 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA----TQ 261
Cdd:COG3096 310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ-EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEArleaAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 262 NTVKELQTCL----QGLELgAAEKEEDYHTALRRLESmlqplAQELeatrdsLDKKNQHLASFPGWLAMAQQKADTASDT 337
Cdd:COG3096 389 EEVDSLKSQLadyqQALDV-QQTRAIQYQQAVQALEK-----ARAL------CGLPDLTPENAEDYLAAFRAKEQQATEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 338 KGRQEPIPSDAAQEMQELGEKLQALERertKVEEVNRQQSAQLEQlvkelQLKEDARaSLERLVKEMAPLQEELSgkgqE 417
Cdd:COG3096 457 VLELEQKLSVADAARRQFEKAYELVCK---IAGEVERSQAWQTAR-----ELLRRYR-SQQALAQRLQQLRAQLA----E 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 418 ADQLWRRLQELlahtssweeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDH 497
Cdd:COG3096 524 LEQRLRQQQNA--------------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 498 LSQQVGMLERLAgppgpelPVAGEKNEALvpvnSSLQEAWGKPEEEQRGLQEA--QLDDTKVQEGSQEEELRQANRELEK 575
Cdd:COG3096 590 LRARIKELAARA-------PAWLAAQDAL----ERLREQSGEALADSQEVTAAmqQLLEREREATVERDELAARKQALES 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 576 ELQNVVGRNQLLEGKLQALQADYQALQQRE-------------SAIQGSLAS------LEAEQASIRHLGDQMEASLL-- 634
Cdd:COG3096 659 QIERLSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfSALYGPARHaivvpdLSAVKEQLAGLEDCPEDLYLie 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 635 --------AVRKAKEAMKAQMA--EKEAILQSKEGEC------------QQLREEVEQcqqLAEaRHRELRALESQCQQQ 692
Cdd:COG3096 739 gdpdsfddSVFDAEELEDAVVVklSDRQWRYSRFPEVplfgraarekrlEELRAERDE---LAE-QYAKASFDVQKLQRL 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 693 TQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLqakmRAALDDQDKVQSQLS-MAEAV 771
Cdd:COG3096 815 HQAFSQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANlLADET 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 772 LREhktLVQQLKEQNEALNRAhVQELLQCSEREGALqEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAEL----Q 847
Cdd:COG3096 891 LAD---RLEELREELDAAQEA-QAFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALsevvQ 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 848 EQLHRANTDTAELGIQVCALTvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSL 927
Cdd:COG3096 966 RRPHFSYEDAVGLLGENSDLN---EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEL 1042
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 928 PGLQAQL-AQAEQRAQSLQEAAHQELNTLKFQLS----------AEIMDYQSRLKNAGEECKSLRGQLEE 986
Cdd:COG3096 1043 EELGVQAdAEAEERARIRRDELHEELSQNRSRRSqlekqltrceAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
267-959 |
3.06e-11 |
|
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: 68.46 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 267 LQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 346
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 347 DA-AQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElsgkgQEADQLWRRL 425
Cdd:TIGR00618 279 LEeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----RRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 426 QELLAhtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVS--QHVSDLEEQKKQLIQDKDHLSQQVG 503
Cdd:TIGR00618 354 EIHIR------------------------------DAHEVATSIREISCQQHTltQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 504 MLERLAGPPGPELpvageknEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKV-QEGSQEE----ELRQANRELEKELQ 578
Cdd:TIGR00618 404 ILQREQATIDTRT-------SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaQCEKLEKihlqESAQSLKEREQQLQ 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 579 NVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGdqmeasllAVRKAKEAMKAQMAEKEAILQSKE 658
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG--------PLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 659 GECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 738
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 739 RLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERAD----- 813
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtll 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 814 -EAQQREEELRALQEELSQAKcSSEEAQLEhAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ---ELQDAK 889
Cdd:TIGR00618 707 rELETHIEEYDREFNEIENAS-SSLGSDLA-AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLA 784
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 890 EAASREREGLERQVAGLQQEKESLQEKLkaaKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQL 959
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQEI---PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1122-1183 |
3.46e-11 |
|
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).
Pssm-ID: 277256 [Multi-domain] Cd Length: 61 Bit Score: 59.66 E-value: 3.46e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvlSKHGGKKERCCRACFQKLS 1183
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKC------SQFLPLHIRCCHHCKDLLE 59
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1122-1179 |
4.20e-11 |
|
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.
Pssm-ID: 277273 [Multi-domain] Cd Length: 61 Bit Score: 59.65 E-value: 4.20e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1179
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHpvRVCDPCA 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
819-1128 |
5.17e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 819 EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERVEealacaVQELQDAKEAASREREG 898
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYE------GYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 899 LERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ-----AEQRAQSLQEAAHqELNTLKFQLSAEIMDYQSRLKNA 973
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 974 GEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTK 1053
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1054 IqeyyNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE-----FQQKLSAEERWLGDTEA 1128
Cdd:TIGR02169 401 I----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqLAADLSKYEQELYDLKE 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-839 |
8.91e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 178 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEVT 257
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 258 QATQNTVKELQtcLQGLELGAAEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 337
Cdd:TIGR02168 424 EELLKKLEEAE--LKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 338 KGRQEPIPSDAAQEMQE----------------------------LGEKLQAL------------------ERERTKVEE 371
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvvenlnaakkaiaflkqnELGRVTFLP 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 372 VNRQQSAQLEQLVKE-LQLKEDARASLERLVKEMAPLQEELSG---------KGQEADQLWRRLQ----------ELLAH 431
Cdd:TIGR02168 578 LDSIKGTEIQGNDREiLKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvdDLDNALELAKKLRpgyrivtldgDLVRP 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 432 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagp 511
Cdd:TIGR02168 658 GGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK---- 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 512 pgpELPVAGEKNEALVPVNSSLQEAWGKPEEeqrglQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKL 591
Cdd:TIGR02168 734 ---DLARLEAEVEQLEERIAQLSKELTELEA-----EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 592 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 671
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 672 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAAQLALSQAQLEVHQGEVQRLQAQV-VDLQAK 750
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSE------LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLT 952
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 751 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvqellqcseregALQEerADEAQQREEELRALQEELS 830
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA-----------------AIEE--YEELKERYDFLTAQKEDLT 1013
|
....*....
gi 1896085763 831 QAKCSSEEA 839
Cdd:TIGR02168 1014 EAKETLEEA 1022
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
736-998 |
1.03e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 736 EVQRLQAQVVDLQAKMRAALDDQDKVQsQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQEllqcSEREGALQEERADEA 815
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLWF----AQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 816 qqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT-AELGIQVCALTVEKERVEEALACAVQELQDAKEAASR 894
Cdd:COG4913 301 ---RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 895 EREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQelntlkfqLSAEIMDYQSRLKNAG 974
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRE--------LEAEIASLERRKSNIP 439
|
250 260
....*....|....*....|....
gi 1896085763 975 EECKSLRGQLEEqgrQLQAAEEAV 998
Cdd:COG4913 440 ARLLALRDALAE---ALGLDEAEL 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
533-948 |
1.15e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 533 LQEAWGKPEEEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQN--VVGRNQLLEGKLQALQADYQALQQRESAIQ 609
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 610 GSLASLEAEQASIRHLGDQMEAsllAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQC 689
Cdd:COG4717 160 ELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 690 ---------QQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALS-------------QAQLEVHQGEVQRLQAQVVDL 747
Cdd:COG4717 237 eaaaleerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllarEKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 748 QAKMRAALDDQDKVQSQLS--MAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEaqqrEEELRAL 825
Cdd:COG4717 317 EEEELEELLAALGLPPDLSpeELLELLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAEAGVED----EEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 826 QEELSQAkcssEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEEALacavQELQDAKEAASREREGLERQVAG 905
Cdd:COG4717 391 LEQAEEY----QELKEELEELEEQLEELLGELEEL-----LEALDEEELEEEL----EELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1896085763 906 LQQEKESLQEKlkaakaaaGSLPGLQAQLAQAEQRAQSLQEAA 948
Cdd:COG4717 458 LEAELEQLEED--------GELAELLQELEELKAELRELAEEW 492
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
190-1056 |
1.30e-10 |
|
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: 66.35 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 190 ELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTC-----------LVAELQKQWEVTQ 258
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAArkqeleeilheLESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 259 ATQNTVKELQTCLQGLElGAAEKEEDYHTALR----RLESMLQPLAQELEATRDSLDKKN-------QHLASFPGWLAMA 327
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLE-EQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSkerklleERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 328 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEevnrQQSAQLEQLVKELQLK-EDARASLERLVKEMAP 406
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----GESTDLQEQIAELQAQiAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 407 LQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQ-FLETQLAQV---SQHVS 482
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAAQQelrSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 483 DLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagEKNEALVPVNSSLqeawgkpeeEQRGLQEAQLDDTKVQEGSQ 562
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQ-------------KHTQALEELTEQL---------EQAKRNKANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 563 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 642
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 643 MKAQMAEKEAILQ-------SKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ-QTQLIEVLTAEKGQQGVGPPTDN 714
Cdd:pfam01576 466 LESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 715 EARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAhv 794
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE---KKQKKFDQMLAEEKAISARY-- 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 795 qellqCSEREGAlqeeradEAQQREEELRALQeeLSQAkcsSEEAQlehaELQEQLHRANTdtaELGIQVCALTVEKERV 874
Cdd:pfam01576 621 -----AEERDRA-------EAEAREKETRALS--LARA---LEEAL----EAKEELERTNK---QLRAEMEDLVSSKDDV 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 875 EEalacAVQELQDAKEAasreregLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQLAQAEQRAQSLQEAAHQELN 953
Cdd:pfam01576 677 GK----NVHELERSKRA-------LEQQVEEMKTQLEELEDELQATEDAKLRLEvNMQALKAQFERDLQARDEQGEEKRR 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 954 TLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA----EEAVEKLKATQADMGEklsctsnHLAECQAAM 1026
Cdd:pfam01576 746 QLVKQvreLEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKD-------LQRELEEAR 818
|
890 900 910
....*....|....*....|....*....|
gi 1896085763 1027 LRKDKEGAALREDlERTQKELEKATTKIQE 1056
Cdd:pfam01576 819 ASRDEILAQSKES-EKKLKNLEAELLQLQE 847
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1122-1178 |
1.61e-10 |
|
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.
Pssm-ID: 277298 [Multi-domain] Cd Length: 71 Bit Score: 58.50 E-value: 1.61e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1178
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1121-1155 |
1.75e-10 |
|
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.
Pssm-ID: 277276 [Multi-domain] Cd Length: 83 Bit Score: 58.67 E-value: 1.75e-10
10 20 30
....*....|....*....|....*....|....*
gi 1896085763 1121 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFC 1155
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVC 35
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
606-1049 |
1.90e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 606 SAIQGSLAS-LEAEQASIRHLGDQMEASLLAVRKAKEAMKaqmaekeaILQSKEGECQQLREEVEQCQQLAEARHRELRA 684
Cdd:PRK04863 211 SAITRSLRDyLLPENSGVRKAFQDMEAALRENRMTLEAIR--------VTQSDRDLFKHLITESTNYVAADYMRHANERR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 685 LESQcqqqtqliEVLTAEKGQQGvgpptdneARElaaQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQ 764
Cdd:PRK04863 283 VHLE--------EALELRRELYT--------SRR---QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 765 LSMAEAVLR---EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEERADEA-------QQREEEL--RALQEElsQA 832
Cdd:PRK04863 344 LRQQEKIERyqaDLEELEERLEEQNEV--VEEADEQQEENEARAEAAEEEVDELksqladyQQALDVQqtRAIQYQ--QA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 833 KCSSEEAQlehaelqEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLE--RQVAG----- 905
Cdd:PRK04863 420 VQALERAK-------QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvRKIAGevsrs 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 906 -LQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEIMDYQS 968
Cdd:PRK04863 493 eAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAerllaefckrlgknldDEDELEQLQEELEARLESLSE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 969 RLKNAGEECKSLRGQLEEQGRQLQ----------AAEEAVEKLkatQADMGEKLScTSNHLAECQAAMLRKDKEGAALRE 1038
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQrlaarapawlAAQDALARL---REQSGEEFE-DSQDVTEYMQQLLERERELTVERD 648
|
490
....*....|.
gi 1896085763 1039 DLERTQKELEK 1049
Cdd:PRK04863 649 ELAARKQALDE 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
461-1008 |
2.98e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 461 RSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAgppgpelpvagEKNEALVPVnsslqeawgkp 540
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE---VLEEHE-----------ERREELETL----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 541 EEEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLA----- 613
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrva 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 614 --SLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL----------AEARHRE 681
Cdd:PRK02224 337 aqAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgnAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 682 LRALESQCQQQTQLIEVlTAEKGQQGVgpptdNEARELAAQLALSQAQLEV----HQGEVQRLQAQVVDLQAKMRAALDD 757
Cdd:PRK02224 417 LREERDELREREAELEA-TLRTARERV-----EEAEALLEAGKCPECGQPVegspHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 758 QDKVQSQLSMAEAvLREHKTLVQQLKEQNEAlnrahVQELLqcseregALQEERADEAQQREEELRALQEEL-SQAKCSS 836
Cdd:PRK02224 491 VEEVEERLERAED-LVEAEDRIERLEERRED-----LEELI-------AERRETIEEKRERAEELRERAAELeAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 837 EEAQLEHAELQEQLHRAntdtAELGIQVCALTVEKERVEeALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEK 916
Cdd:PRK02224 558 EAAAEAEEEAEEAREEV----AELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 917 LKAAKAAAGSLPGLQAQLAQAE-QRAQSLQEAAHQELNTL---KFQLSAEIMDYQSRLKNAgEECKSLRGQLEEQGRQLQ 992
Cdd:PRK02224 633 RERKRELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEEL-EELRERREALENRVEALE 711
|
570
....*....|....*.
gi 1896085763 993 AAEEAVEKLKATQADM 1008
Cdd:PRK02224 712 ALYDEAEELESMYGDL 727
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1122-1182 |
4.44e-10 |
|
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.
Pssm-ID: 277294 [Multi-domain] Cd Length: 64 Bit Score: 56.97 E-value: 4.44e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 1122 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1182
Cdd:cd15755 2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSeKKFLLPSQSSKPVRVCDFCYDLL 64
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1122-1180 |
4.48e-10 |
|
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.
Pssm-ID: 277263 [Multi-domain] Cd Length: 61 Bit Score: 56.75 E-value: 4.48e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 1122 WLGDTEANHCLDCKRE-FSWMVRRHHCRICGRIFCYYCCNNYVL-SKHGGKKERCCRACFQ 1180
Cdd:cd15724 1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLvEGYRENPVRVCDQCYE 61
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
773-1050 |
5.06e-10 |
|
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: 64.59 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 773 REHKTLVQQLKEQNEALNRAhVQELLQCSEREGALQEE---------------RADEA-QQREEELRALQEELSQAKCSS 836
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEM-ARELEELSARESDLEQDyqaasdhlnlvqtalRQQEKiERYQEDLEELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 837 EEAQLEHAELQEQLHRANTDTAELGIQVC----ALTVEKER----------VEEALAC---------------------- 880
Cdd:COG3096 371 EEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqALDVQQTRaiqyqqavqaLEKARALcglpdltpenaedylaafrake 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 881 ---------AVQELQDAKEAASREREGLE--RQVAG-------LQQEKESLqEKLKAAKAAAGSLPGLQAQLAQAEQRAQ 942
Cdd:COG3096 451 qqateevleLEQKLSVADAARRQFEKAYElvCKIAGeversqaWQTARELL-RRYRSQQALAQRLQQLRAQLAELEQRLR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 943 SLQEA----------------AHQELNTLKFQLSAEIMDYQSRLKNAGE---ECKSLRGQLEEQGRQLQAAEEAVEKLKA 1003
Cdd:COG3096 530 QQQNAerlleefcqrigqqldAAEELEELLAELEAQLEELEEQAAEAVEqrsELRQQLEQLRARIKELAARAPAWLAAQD 609
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1004 TQADMGEKLSCTSNHLAECQAAM---LRKDKEGAALREDLERTQKELEKA 1050
Cdd:COG3096 610 ALERLREQSGEALADSQEVTAAMqqlLEREREATVERDELAARKQALESQ 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
515-1128 |
5.66e-10 |
|
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: 64.32 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 515 ELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANrELEKELQNVVGRNQLLEGKLQAL 594
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKE-ALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 595 QADYQALQQRESAIQGSLASLEAEqasIRHLGdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL 674
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKK---IKDLG---EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 675 AEARHRELRALESQCQQQTQLIEVLTAE-KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRA 753
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 754 ALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALN---RAHVQELLQCSE-REGALQEERADEAQQR--EEELRALQE 827
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAAdLSKYEQELYDLKEEYDrvEKELSKLQR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 828 ELSQAkcsseEAQLEHAELQEQLHRANTDTAELGIQ-VCALTVEKERVEEALACAVQ-----ELQ----DAKEAASRERE 897
Cdd:TIGR02169 491 ELAEA-----EAQARASEERVRGGRAVEEVLKASIQgVHGTVAQLGSVGERYATAIEvaagnRLNnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 898 GLERQVAGLQ--------QEKESLQEKLKAAKAAA--------------------------------------------- 924
Cdd:TIGR02169 566 LLKRRKAGRAtflplnkmRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtle 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 925 ------------GSLPGLQAQLAQAEQRAQSLQEAAH-QELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 991
Cdd:TIGR02169 646 gelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 992 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEK--------ATTKIQEYYNKLCQ 1063
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlshsRIPEIQAELSKLEE 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1064 EVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALwqKSDALEFQQKLSAEERWLGDTEA 1128
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL--KEQIKSIEKEIENLNGKKEELEE 868
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1122-1179 |
9.28e-10 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.
Pssm-ID: 277282 [Multi-domain] Cd Length: 61 Bit Score: 55.91 E-value: 9.28e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN-YVLSKHGGKKERCCRACF 1179
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNkAPLEYLKNKSARVCDECF 61
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
355-1002 |
1.06e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 355 LGEKLQALERERTKVEEVnRQQSAQLEQLVKElqlKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtss 434
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKF-IKRTENIEELIKE---KEKELEEVLREINEISSELPELREELEKLEKEVKELEEL------ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 435 weeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQliqdkdhlsqqvgmLERLAGPPGP 514
Cdd:PRK03918 237 --------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------------LKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 515 ELPVAGEKNEALVPVNsSLQEAWGKPEEEQRGLQEaqlddtKVQEGSQEEELRQANRELEKELQNVVGRnqlLEGKLQAL 594
Cdd:PRK03918 295 YIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEE------RIKELEEKEERLEELKKKLKELEKRLEE---LEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 595 QaDYQALQQRESAIQGSLASLEAEQAsirhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEqcqql 674
Cdd:PRK03918 365 E-EAKAKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 675 aearhrELRALESQCQQQTQLIevltaekgqqgvgppTDNEARELaaqlalsqaqLEVHQGEVQRLQAQVVDLQAKMRAA 754
Cdd:PRK03918 430 ------ELKKAKGKCPVCGREL---------------TEEHRKEL----------LEEYTAELKRIEKELKEIEEKERKL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 755 LDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALNRAHVQELlqcsEREGALQEERADEAQQREEELRALQEELSQAK- 833
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEe 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 834 CSSEEAQLEHA--ELQEQLHRANTDTAELGIQvcALTVEKERVEEaLACAVQELQDAKEAASREREGLERqvagLQQEKE 911
Cdd:PRK03918 554 LKKKLAELEKKldELEEELAELLKELEELGFE--SVEELEERLKE-LEPFYNEYLELKDAEKELEREEKE----LKKLEE 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 912 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRaqsLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 991
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKK---YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
650
....*....|.
gi 1896085763 992 QAAEEAVEKLK 1002
Cdd:PRK03918 704 EEREKAKKELE 714
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
563-1057 |
1.34e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 563 EEELRQANRELEKE----LQNVVGRNQLLEGKLQALQ---ADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEA--SL 633
Cdd:COG4717 48 LERLEKEADELFKPqgrkPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 634 LAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhrELRALESQCQQQTQLIEVLTAEKGQQgvgppTD 713
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQD-----LA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 714 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAlDDQDKVQSQLSMAEAVLRehkTLVQQLKEQNEALNRAH 793
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAA---LLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 794 VQELLQcseregALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtAELGIqvcALTVEKER 873
Cdd:COG4717 275 IAGVLF------LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-------AALGL---PPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 874 VEEALAcAVQELQDAKEAASREREglERQVAGLQQEKESLQEKLKAAKAaagslpglqAQLAQAEQRAQSLQEAAhQELN 953
Cdd:COG4717 339 LLELLD-RIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVEDE---------EELRAALEQAEEYQELK-EELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 954 TLKFQLSAEIMDYQSRLKNAGEEckSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSctsnhlaecqaaMLRKDKEG 1033
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELE------------QLEEDGEL 471
|
490 500
....*....|....*....|....
gi 1896085763 1034 AALREDLERTQKELEKATTKIQEY 1057
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAAL 495
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1119-1182 |
1.60e-09 |
|
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.
Pssm-ID: 277267 [Multi-domain] Cd Length: 63 Bit Score: 55.12 E-value: 1.60e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 1119 EERWlgdTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACFQKL 1182
Cdd:cd15728 1 EPPW---ADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCsTKEVPIIKFDlNKPVRVCDVCFDVL 63
|
|
| FYVE_FGD1_2_4 |
cd15741 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ... |
1121-1182 |
1.63e-09 |
|
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.
Pssm-ID: 277280 [Multi-domain] Cd Length: 65 Bit Score: 55.19 E-value: 1.63e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 1121 RWLGDTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACFQKL 1182
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFNALTrRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1122-1182 |
2.58e-09 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.
Pssm-ID: 277259 [Multi-domain] Cd Length: 65 Bit Score: 54.70 E-value: 2.58e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACFQKL 1182
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFesEIRRLRISRPVRVCQACYNIL 65
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
344-1120 |
2.83e-09 |
|
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: 61.91 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 344 IPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLE--------RLVKEMAPLQEELSGKG 415
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkeklELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 416 QEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDK 495
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 496 DHLSQQVGMLERLagppgpelpvagEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEK 575
Cdd:pfam02463 317 KESEKEKKKAEKE------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 576 ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR----------HLGDQMEASLLAVRKAKEAMKA 645
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILeeeeesielkQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 646 QMAEKEAILQSKEGECQQLREEVEQC--QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQL 723
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 724 ALSQAQLEVHQGEVQRLQAQVvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLvqqlkEQNEALNRAHVQELLQCSER 803
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQK--LVRALTELPLGARKLRLLIPKLKLPLKSIAVL-----EIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 804 EGALQEERADeaqQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ 883
Cdd:pfam02463 618 DDKRAKVVEG---ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 884 ELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEI 963
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 964 MDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQAAMLRKDKEGAALREDLERT 1043
Cdd:pfam02463 775 ELAEEREKT---EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE------QLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 1044 QKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1120
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
|
| RUN_RUNDC3A |
cd17699 |
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ... |
33-139 |
4.57e-09 |
|
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.
Pssm-ID: 439061 Cd Length: 151 Bit Score: 56.57 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGN--KKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17699 20 EPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSdgQRGFWDYIRLACSKV--PNNCISSIENMENISTSRAKGRAWIRV 97
|
90 100
....*....|....*....|....*....
gi 1896085763 111 SLVHQRLADTLQQCFMNTKVTRRTLTTGS 139
Cdd:cd17699 98 ALMEKRLSEYIATALRDTRTTRRFYDDGA 126
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1126-1179 |
4.71e-09 |
|
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.
Pssm-ID: 277274 [Multi-domain] Cd Length: 59 Bit Score: 53.69 E-value: 4.71e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 1126 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1179
Cdd:cd15735 4 VDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQpvRVCDGCY 59
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1131-1179 |
4.98e-09 |
|
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.
Pssm-ID: 277288 [Multi-domain] Cd Length: 51 Bit Score: 53.28 E-value: 4.98e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1131 CLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACF 1179
Cdd:cd15749 2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTfSAVVPRKGNQKQKVCKQCH 51
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
548-1056 |
6.01e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 548 QEAQLDDTKVQ-EGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLg 626
Cdd:PRK02224 185 QRGSLDQLKAQiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 627 dqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVE---QCQQLAEARHRELRALESQCQQQTQLIEVLTAEK 703
Cdd:PRK02224 264 ---RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 704 GQQGVGPPTD------------NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAV 771
Cdd:PRK02224 341 NEEAESLREDaddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL---EEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 772 LREHKTLVQQLKE-----QNEALNRAHVQELL---QCSEREGALQE-ERADEAQQREEELRALQEELsqakcssEEAQLE 842
Cdd:PRK02224 418 REERDELREREAEleatlRTARERVEEAEALLeagKCPECGQPVEGsPHVETIEEDRERVEELEAEL-------EDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 843 HAELQEQLHRAnTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 922
Cdd:PRK02224 491 VEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 923 AAGSLPGLQAQLAQAEQRAQSLqeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1002
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESL----------------ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 1003 ATQADMGEKLSctsnhlaecqaamlrkDKEGAALREDLERTQKELEKATTKIQE 1056
Cdd:PRK02224 634 ERKRELEAEFD----------------EARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
542-908 |
6.64e-09 |
|
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: 60.74 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 542 EEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQA----LQADYQALQQRESaiqgslasL 615
Cdd:COG3096 278 NERRELSERALELRRELFGARRQlaEEQYRLVEMARELEELSARESDLEQDYQAasdhLNLVQTALRQQEK--------I 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 616 EAEQASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------LRALEsQ 688
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAE----QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqaVQALE-K 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 689 CQQQTQLIEvLTAE-----------KGQQGvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQA----- 742
Cdd:COG3096 425 ARALCGLPD-LTPEnaedylaafraKEQQA-----TEEVLELEQKLSVADAARRQFEkayelvckiaGEVERSQAwqtar 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 743 QVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNR-------------AHVQELLQCSEREGALQE 809
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQqldaaeeleellaELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 810 ERAdEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERveealacavqELQDAK 889
Cdd:COG3096 579 QRS-ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV-TAAMQQLLERER----------EATVER 646
|
410
....*....|....*....
gi 1896085763 890 EAASREREGLERQVAGLQQ 908
Cdd:COG3096 647 DELAARKQALESQIERLSQ 665
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
463-1116 |
7.72e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 463 LTRQLQFLETQLAQVSQH---VSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvaGEKNEALVPVNSSLQEAWGK 539
Cdd:PRK04863 319 LNEAESDLEQDYQAASDHlnlVQTALRQQEKIERYQADL---------------------EELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 540 PEEEQRGLQEAQL--DDTK-----VQEGSQEEELR-----QANRELEK----------ELQNVVGRNQLLEGKLQALQAD 597
Cdd:PRK04863 378 QEENEARAEAAEEevDELKsqladYQQALDVQQTRaiqyqQAVQALERakqlcglpdlTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 598 YQALQQRESAIQGSLASLEAEQASIRHLGDQMEASlLAVRKAKEAmkaqmaekeailqskegeCQQLREEVEQCQQLaEA 677
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS-EAWDVAREL------------------LRRLREQRHLAEQL-QQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 678 RHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLalsQAQLEVHQGEvqrlQAQVVDLQAKMRAALDD 757
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL---EARLESLSES----VSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 758 QDKVQSQLSMAEAVLREHKTLVQQLKEQNEA--LNRAHVQELLQ-CSEREGALQEERaDEAQQREEELRALQEELSQAKC 834
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEefEDSQDVTEYMQqLLERERELTVER-DELAARKQALDEEIERLSQPGG 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 835 SSEEAQLEHAE------LQE-----QLHRANTDTAELGIQVCALTV-EKERVEEALA----C------------------ 880
Cdd:PRK04863 670 SEDPRLNALAErfggvlLSEiyddvSLEDAPYFSALYGPARHAIVVpDLSDAAEQLAgledCpedlyliegdpdsfddsv 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 881 -AVQELQDA--KEAASRE-------------REGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSL 944
Cdd:PRK04863 750 fSVEELEKAvvVKIADRQwrysrfpevplfgRAAREKRIEQLRAEREELAERY--------------ATLSFDVQKLQRL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 945 QEAAHQELNT---LKFQL--SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM--------GEK 1011
Cdd:PRK04863 816 HQAFSRFIGShlaVAFEAdpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1012 LSCTSNHLAECQAAMLRKDKEGAALR-------------EDLERTQKELEKATTKIQEYYNK---LCQEVTNRE----RN 1071
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAhfsyED 975
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1072 DQKMLADLDDLN-RTKKYLEERLIELLRDKDALWQK----SDALEFQQKL 1116
Cdd:PRK04863 976 AAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQVLASL 1025
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
719-946 |
8.66e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 719 LAAQLALSQAQLEVHQGEVQRLQAQ--VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNeALNRAHVQE 796
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-GSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 797 LLQcSEREGALQEERADEAQQREEELRALQEELSQAKcsseeaqlehaELQEQLhrantdtaelgiqvcaltvekERVEE 876
Cdd:COG3206 259 LLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVI-----------ALRAQI---------------------AALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 877 ALAcavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKaakaaagSLPGLQAQLAQAEQRAQSLQE 946
Cdd:COG3206 306 QLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLA-------ELPELEAELRRLEREVEVARE 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
672-916 |
1.49e-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: 58.62 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 672 QQLAEARHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 751
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-------------KALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 752 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcSEREGALQEERADEAQQREEELRALQEELSQ 831
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 832 AKcssEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 911
Cdd:COG4942 165 LR---AELEAERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 1896085763 912 SLQEK 916
Cdd:COG4942 238 AAAER 242
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1122-1182 |
2.91e-08 |
|
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.
Pssm-ID: 277293 [Multi-domain] Cd Length: 64 Bit Score: 51.88 E-value: 2.91e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 1122 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1182
Cdd:cd15754 2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRqRFLIPRLSPKPVRVCSLCYRKL 64
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
186-917 |
3.13e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 186 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQG--EQLQTERERGRTAAEDNVRLTCLVAELQKQWEV-TQATQN 262
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLEEQNEVVEEADEQQEENEArAEAAEE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 263 TVKELQTCL----QGLELgAAEKEEDYHTALRRLESM-----LQPLAQE-LEATRDSLDKKNQHLASFpgwLAMAQQKAD 332
Cdd:PRK04863 391 EVDELKSQLadyqQALDV-QQTRAIQYQQAVQALERAkqlcgLPDLTADnAEDWLEEFQAKEQEATEE---LLSLEQKLS 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 333 TASDTKGRQE-----------PI-PSDAAQEMQEL----------GEKLQALERERTKVEEVNRQQsAQLEQLVKEL--- 387
Cdd:PRK04863 467 VAQAAHSQFEqayqlvrkiagEVsRSEAWDVARELlrrlreqrhlAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFckr 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 388 ------------QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekel 455
Cdd:PRK04863 546 lgknlddedeleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD--------------- 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 456 leqevrSLTR-QLQFLETQL--AQVSQHVSDLEEQKKQLIQDKDHLSQQVGML----ERLAGPPGPELPVAGEKNEALVP 528
Cdd:PRK04863 611 ------ALARlREQSGEEFEdsQDVTEYMQQLLERERELTVERDELAARKQALdeeiERLSQPGGSEDPRLNALAERFGG 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 529 VnsSLQEAWgkpeeeqrglqeaqlDDTKVQEGSQEE----ELRQA--NRELEKELQNVVGRNQLLEgKLQALQADYQALQ 602
Cdd:PRK04863 685 V--LLSEIY---------------DDVSLEDAPYFSalygPARHAivVPDLSDAAEQLAGLEDCPE-DLYLIEGDPDSFD 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 603 QresaiqGSLASLEAEQASIRHLGD-QMEAS------LLAvRKAKEAmkaQMAEKEAILQSKEGECQQLREEVEQCQQLA 675
Cdd:PRK04863 747 D------SVFSVEELEKAVVVKIADrQWRYSrfpevpLFG-RAAREK---RIEQLRAEREELAERYATLSFDVQKLQRLH 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 676 EA------------------------------RHRELRALESQCQQQTQLIEvlTAEKGQQGVG-----------PPTDN 714
Cdd:PRK04863 817 QAfsrfigshlavafeadpeaelrqlnrrrveLERALADHESQEQQQRSQLE--QAKEGLSALNrllprlnlladETLAD 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 715 EARELAAQLA-LSQAQLEVHQGevQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEalNRAH 793
Cdd:PRK04863 895 RVEEIREQLDeAEEAKRFVQQH--GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAH 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 794 ------VQELLQCSEREGALQEERADEAQQRE---EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQV 864
Cdd:PRK04863 971 fsyedaAEMLAKNSDLNEKLRQRLEQAEQERTrarEQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 865 CaltvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 917
Cdd:PRK04863 1051 D------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1131-1182 |
3.86e-08 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277281 [Multi-domain] Cd Length: 67 Bit Score: 51.47 E-value: 3.86e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 1131 CLDCKREFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1182
Cdd:cd15742 12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAEL 64
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
186-850 |
5.14e-08 |
|
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: 57.67 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 186 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVK 265
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT-QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 266 ELQTCLQglELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLAsfpgwlAMAQQKADTASDTKgrqepip 345
Cdd:TIGR00618 281 ETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA------AHVKQQSSIEEQRR------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 346 sdAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElSGKGQEADQLWRRL 425
Cdd:TIGR00618 346 --LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE-QATIDTRTSAFRDL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 426 QELLAHTSSWEEELAELRREKKQ----QQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQ 501
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 502 VGMLERLAGPPGPELPVAGEKNEALVPV---------------------NSSLQEAWGKPEEEQRGLQEAQLDDTKVQEG 560
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqletseedvyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 561 SQE--------EELRQANRELEKELQNVVGRNQLLEGKLQALQADYQA---LQQRESAIQGSLASLEAEQASIrhLGDQM 629
Cdd:TIGR00618 583 KEDipnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhLQQCSQELALKLTALHALQLTL--TQERV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 630 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLievltaekgqqgvg 709
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA-------------- 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 710 pptdneareLAAQLALSQAQLEVHQGEVQRLQAQvvdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAL 789
Cdd:TIGR00618 727 ---------SSSLGSDLAAREDALNQSLKELMHQ-------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 790 NRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQL 850
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1131-1179 |
6.27e-08 |
|
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.
Pssm-ID: 277275 [Multi-domain] Cd Length: 56 Bit Score: 50.64 E-value: 6.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1131 CLDCKREFSWMVRRHHCRICGRIFC-YYCCNNYVLSKHG-----GKKERCCRACF 1179
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCrRHLPNMIPLNLSAydprnGKWYRCCHSCF 56
|
|
| RUN_RUNDC3B |
cd17700 |
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ... |
33-139 |
6.65e-08 |
|
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.
Pssm-ID: 439062 Cd Length: 151 Bit Score: 53.43 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 33 EPITDDSTSLHKFSYKLEYLLQFDQKEKATLLG--NKKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRY 110
Cdd:cd17700 20 ETIDDSSPEFVNFAAILEQILSHRLKGQVTWFGyeSPRSFWDYIRVACSKV--PHNCICSIENMENVSSSRAKGRAWIRV 97
|
90 100
....*....|....*....|....*....
gi 1896085763 111 SLVHQRLADTLQQCFMNTKVTRRTLTTGS 139
Cdd:cd17700 98 ALMEKRLSEYISTALRDFKTTRRFYEDGA 126
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-984 |
7.06e-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: 56.31 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 719 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahvqELL 798
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 799 QCSEREGALQEERADEAQQREEELRALQEelsqakcSSEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEAL 878
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYR-------LGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 879 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAhQELNTLKFQ 958
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEA-EELEALIAR 231
|
250 260
....*....|....*....|....*.
gi 1896085763 959 LSAEIMDYQSRLKNAGEecKSLRGQL 984
Cdd:COG4942 232 LEAEAAAAAERTPAAGF--AALKGKL 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
531-1120 |
7.45e-08 |
|
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: 57.16 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 531 SSLQEAWGKPEEEQRGL--QEAQLDDTKVQEGSQEEELRQanrELEKELQNVVGRNQLLEGKLQALQADYQALQQ-RESA 607
Cdd:pfam12128 311 SAADAAVAKDRSELEALedQHGAFLDADIETAAADQEQLP---SWQSELENLEERLKALTGKHQDVTAKYNRRRSkIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 608 IQGSLASLEAEQASIRhlgdqmeasllavrkakEAMKAQMAEKEAILQskeGECQQLREEVEQcqQLAEARhrelrales 687
Cdd:pfam12128 388 NNRDIAGIKDKLAKIR-----------------EARDRQLAVAEDDLQ---ALESELREQLEA--GKLEFN--------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 688 qcQQQTQLIEVLTAEKGQQGVGPPTDnearELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSM 767
Cdd:pfam12128 437 --EEEYRLKSRLGELKLRLNQATATP----ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 768 AEAVLREHKTLVQQLKEQNEAlnRAHvqELLQCSEREGALQEERADEAQQREEELRA-LQEELSQAKCSSEEA------- 839
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFP--QAG--TLLHFLRKEAPDWEQSIGKVISPELLHRTdLDPEVWDGSVGGELNlygvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 840 --QLEH---AELQEQLhRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLE-------RQVAGLQ 907
Cdd:pfam12128 587 lkRIDVpewAASEEEL-RERLDKAEEALQ--SAREKQAAAEEQLVQANGELEKASREETFARTALKnarldlrRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 908 QEKESLQEKLKaakaaagslpglqAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEImdyqsrlknageeckslRGQLEEQ 987
Cdd:pfam12128 664 SEKDKKNKALA-------------ERKDSANERLNSLEAQLKQLDKKHQ-AWLEEQ-----------------KEQKREA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 988 GRQLQAAEEAVEKLKATQADM--GEKLSCTSNHLAECQAAMLRKDKEGAAL-------------REDLERTQKELEKATT 1052
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkreIRTLERKIERIAVRRQ 792
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 1053 KIQEYYNKLcQEVTNRERndQKMLADLDDLNRTKKYLEERLIELL----RDKDALWQKSDALEFQQKLSAEE 1120
Cdd:pfam12128 793 EVLRYFDWY-QETWLQRR--PRLATQLSNIERAISELQQQLARLIadtkLRRAKLEMERKASEKQQVRLSEN 861
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
352-876 |
9.82e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 352 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAH 431
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 432 TSSWEEElaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLiqdkDHLSQQVGMLERlagp 511
Cdd:COG4717 128 LPLYQEL----------------------EALEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQE---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 512 pgpelpvagEKNEALVPVNSSLQEAWGKPEEEQrglqeaqlddtkvqegsqeEELRQANRELEKELQNVVGRNQLLEGKL 591
Cdd:COG4717 178 ---------ELEELLEQLSLATEEELQDLAEEL-------------------EELQQRLAELEEELEEAQEELEELEEEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 592 QALQADYQALQQRES-AIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ 670
Cdd:COG4717 230 EQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 671 CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQL--ALSQAQLEVHQGEVQRLQAQVvdlQ 748
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE------ELQELLREAeeLEEELQLEELEQEIAALLAEA---G 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 749 AKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEAQQRE---EELRAL 825
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEelrEELAEL 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 826 QEELSQAKCSSE--EAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEE 876
Cdd:COG4717 459 EAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-917 |
1.17e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 171 DLNSPLNNEALEGFDEMRLELDQLEVREkqlrerMQQLDRENQ-----ELRAAVSQQGEQLQTERERGRTAAEDNVRLTC 245
Cdd:PTZ00121 1019 DFNQNFNIEKIEELTEYGNNDDVLKEKD------IIDEDIDGNhegkaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 246 LVAELQKQWEVTQATQNTVKELQTCLQglelgAAEKEEDYHTA--LRRLESmlqplAQELEATRDSLDKKNQHLASfpgw 323
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEE-----AKKKAEDARKAeeARKAED-----ARKAEEARKAEDAKRVEIAR---- 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 324 lamAQQKADTASDTKGRQEPIPSDAAQEMQELGEKlqaleRERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 403
Cdd:PTZ00121 1159 ---KAEDARKAEEARKAEDAKKAEAARKAEEVRKA-----EELRKAEDARKAEAARKAEEERKA---EEARKAEDAKKAE 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 404 MAPLQEELSGKGQEAdqlwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSD 483
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEA----KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 484 LEEQKKQLIQDK--DHLSQQVGMLERLAGPPGPELPVAGEKNEAlvpvnsSLQEAWGKPEEEQRGLQEAQLDDTKVQEGS 561
Cdd:PTZ00121 1304 ADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEA------AKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 562 QE--------EELRQANrELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA----SIRHLGDQM 629
Cdd:PTZ00121 1378 KKadaakkkaEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadEAKKKAEEA 1456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 630 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV----EQCQQLAEARHR--ELRALES--------QCQQQTQL 695
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEAKKAAEAKKKadEAKKAEEakkadeakKAEEAKKA 1536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 696 IEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLR-- 773
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKae 1616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 774 EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEE----------RADEAQQREEELRALQEELSQA---KCSSEEAQ 840
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEElkkaeeenkiKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 841 LEHAELQ---EQLHRANTDTAELGIQV-CALTVEKERVEEALACAVQELQDAKEAasREREGLERQVAGLQQEKESLQEK 916
Cdd:PTZ00121 1695 KKEAEEAkkaEELKKKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772
|
.
gi 1896085763 917 L 917
Cdd:PTZ00121 1773 I 1773
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
340-1042 |
1.52e-07 |
|
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: 56.34 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 340 RQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLK-------EDARASLERLVKEMAPLQEELS 412
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcaeaEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 413 GKGQEADQLWRRLQ----ELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQK 488
Cdd:pfam01576 82 SRLEEEEERSQQLQnekkKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 489 KQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE------AQLDDTKVQEGSQ 562
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiaelqAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 563 EEELRQANRELEKElqnvVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQasiRHLGDQMEasllAVRKAKEA 642
Cdd:pfam01576 242 EEELQAALARLEEE----TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR---RDLGEELE----ALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 643 MKAQMAEKEAILQSKEGECQQLREEVEQ-----CQQLAEARHRELRALESQCQQQTQLIEVLTA-EKGQQGVgpptDNEA 716
Cdd:pfam01576 311 TLDTTAAQQELRSKREQEVTELKKALEEetrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANlEKAKQAL----ESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 717 RELAAQL-ALSQAQLEVHQGEvQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQ 795
Cdd:pfam01576 387 AELQAELrTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 796 ELLQCSEREGALQEER------ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTV 869
Cdd:pfam01576 466 LESQLQDTQELLQEETrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 870 EKERVEEALACAVQELQDAKEAASReregLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ--AEQRAQSLQ-- 945
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlAEEKAISARya 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 946 ------EAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEE-------QGRQLQAAEEAVEKLKATQADMGEKL 1012
Cdd:pfam01576 622 eerdraEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDlvsskddVGKNVHELERSKRALEQQVEEMKTQL 701
|
730 740 750
....*....|....*....|....*....|
gi 1896085763 1013 SCTSNHLAECQAAMLRKDKEGAALREDLER 1042
Cdd:pfam01576 702 EELEDELQATEDAKLRLEVNMQALKAQFER 731
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
558-784 |
1.53e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 558 QEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQ--ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 635
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 636 VRKAKEAMKAQMAE--KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptd 713
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------------- 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 714 neaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE 784
Cdd:COG3206 309 ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
465-841 |
1.99e-07 |
|
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: 56.11 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 465 RQLQFLETQLAQVSQHVSDLEEQKKQLIQD----KDHLS------QQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQ 534
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 535 EAwgkpeEEQRGLQEAQLDDTKVQEGSQEEEL----------RQANRELEKElQNVVGRNQL----LEGKLQALQADYQA 600
Cdd:COG3096 379 EA-----EARLEAAEEEVDSLKSQLADYQQALdvqqtraiqyQQAVQALEKA-RALCGLPDLtpenAEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 601 LQQRESAIQGSLASLEAEQAsirhlgdQMEASLLAVRKAKEAMKAQMAEKEAIlqskegecQQLREEVEQCQQLA----- 675
Cdd:COG3096 453 ATEEVLELEQKLSVADAARR-------QFEKAYELVCKIAGEVERSQAWQTAR--------ELLRRYRSQQALAQrlqql 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 676 EARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAL 755
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQ----------LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 756 DDQDKVQSQLSMAEAVLREHKTLVQQLKEQ-NEAL-NRAHVQELLQCS-EREGALQEERaDEAQQREEELRALQEELSQA 832
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALERLREQsGEALaDSQEVTAAMQQLlEREREATVER-DELAARKQALESQIERLSQP 666
|
....*....
gi 1896085763 833 KcSSEEAQL 841
Cdd:COG3096 667 G-GAEDPRL 674
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
325-1060 |
2.20e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 325 AMAQQKAD-TASDTKGRQEPIPSDAAQEMQELGEKLQALER--ERTKVEEVNRQQSAQLEQLVKELQlkEDARASLERLV 401
Cdd:PTZ00121 1083 AKEDNRADeATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAE--DAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 402 KEMAplQEELSGKGQEAdqlwRRLQEllAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHV 481
Cdd:PTZ00121 1161 EDAR--KAEEARKAEDA----KKAEA--ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 482 SDL---EEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGE---KNEALVPVNSSLQEAWGKPEEEQRGLQEAQlddT 555
Cdd:PTZ00121 1233 EEAkkdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearKADELKKAEEKKKADEAKKAEEKKKADEAK---K 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 556 KVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 635
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 636 VRKAKEAMK--------AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQtqliEVLTAEKGQQG 707
Cdd:PTZ00121 1390 KKKADEAKKkaeedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----EAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 708 VGPPTDNEARELAAQLALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK---E 784
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeE 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 785 QNEALNRAHVQELLQCSEREGALQEERADE---------------AQQREEELRALQEELSQAKCSSEEAQLEHAELQEQ 849
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalrkaeeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 850 LHRANTDTAELGIQVCALTVEKERVEEAL----ACAVQELQDAKEAASREREGLERQVAglQQEKESLQEKLKAAKAAAG 925
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeeENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 926 SLPGLQAQLAQAEQRAQSLQEAahQELNTLKfqlsaeimdyqsrlknaGEECKslRGQLEEQGRQLQAAEEAVEKLKATQ 1005
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKA--EEENKIK-----------------AEEAK--KEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1006 ADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK 1060
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
812-1051 |
2.23e-07 |
|
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: 54.77 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 812 ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvekerveeALACAVQELQDAKEA 891
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------------------ALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 892 ASREREGLERQVAGLQQEKESLQEKLKA---AKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQS 968
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 969 RLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1048
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1896085763 1049 KAT 1051
Cdd:COG4942 241 ERT 243
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1122-1179 |
2.39e-07 |
|
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277277 [Multi-domain] Cd Length: 61 Bit Score: 48.86 E-value: 2.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1122 WLGDTEANHClDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKH-GGKKERCCRACF 1179
Cdd:cd15738 3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRaLPGHlSQRPVPVCRACY 61
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
388-642 |
2.56e-07 |
|
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: 54.77 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 388 QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtssweeelaelrrekkqqqeekellEQEVRSLTRQL 467
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----------------------------ERRIAALARRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 468 QFLETQLAQVSQHVSDLEEQ----KKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAwgkpeEE 543
Cdd:COG4942 72 RALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----AP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 544 QRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR 623
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*....
gi 1896085763 624 HLGDQMEASLLAVRKAKEA 642
Cdd:COG4942 227 ALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
542-754 |
3.80e-07 |
|
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: 54.00 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 542 EEQRGLQEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAE 618
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 619 QASIRHLG-----------DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALES 687
Cdd:COG4942 113 LYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 688 QCQQQTQLIevltaekgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAA 754
Cdd:COG4942 193 LKAERQKLL--------------------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
801-1119 |
3.94e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 801 SEREGALQEERADEAQQREEELRALQEELSQaKCSSEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEE--AL 878
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLES-ELAELDEEIERYEEQREQARETRDEADE-----VLEEHEERREEleTL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 879 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG----SLPGLQAQLAQAEQRAQSLQE------AA 948
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRDrleecrVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 949 HQELNTLKFQLSAEIMDYQSRLKNAGEECKSL-------RGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAE 1021
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELeseleeaREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1022 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLC-QEVTNRERNDQkmladLDDLNRTKKYLEERLIELLRDK 1100
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKCPECgQPVEGSPHVET-----IEEDRERVEELEAELEDLEEEV 491
|
330
....*....|....*....
gi 1896085763 1101 DALWQKSDALEFQQKLSAE 1119
Cdd:PRK02224 492 EEVEERLERAEDLVEAEDR 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
193-549 |
4.25e-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: 54.69 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 193 QLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRltclvaELQKQWEVTQATQNTVKELQTclq 272
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIG------EIEKEIEQLEQEEEKLKERLE--- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 273 glelgaaekeedyhtalrRLESMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKGRQEPIPSDAAQEM 352
Cdd:TIGR02169 741 ------------------ELEEDLSSLEQEIENVKSELKELEARI---------EELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 353 QELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEmapLQEELSGKGQEADQLWRRLQELLAHT 432
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 433 SSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlagPP 512
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----EI 946
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 513 GPELPVAG----------EKNEALVPVN--------------SSLQEAWGKPEEEQRGLQE 549
Cdd:TIGR02169 947 PEEELSLEdvqaelqrveEEIRALEPVNmlaiqeyeevlkrlDELKEKRAKLEEERKAILE 1007
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
891-1129 |
4.41e-07 |
|
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: 54.00 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 891 AASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQAQLAQAEQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRL 970
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 971 KNAGEECKSLRGQLEEQGRQLQAAEEAVE-KLKATQAD------MGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERT 1043
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1044 QKELEKATTKIQEYYNKLCQEVTNRERNdqkmladLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEERWL 1123
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 1896085763 1124 GDTEAN 1129
Cdd:COG4942 246 AGFAAL 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
268-915 |
5.97e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 268 QTCLQGLELGAAEKEE-DYHTALRRLEsmlqplaQELEATRDSLDKKNqhlasfpgwlamaqQKADTASDTKGRQEPIPS 346
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEkDLHERLNGLE-------SELAELDEEIERYE--------------EQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 347 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLvkelqlkEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQ 426
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEV-------RDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 427 EllahtssweeelaelrrekkqqqeekelleqevrsLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmle 506
Cdd:PRK02224 318 E-----------------------------------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 507 rlagppgpelpvAGEKnealvpvnsslqeawgkpeEEQRGLQEAQLDDTKVQEGSQEEELrqanRELEKELQNVVGRNQL 586
Cdd:PRK02224 358 ------------AEEL-------------------REEAAELESELEEAREAVEDRREEI----EELEEEIEELRERFGD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 587 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgdqmeasllAVRKAKEAMKAqmaekeailqSKEGECQQLRE 666
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARE----------RVEEAEALLEA----------GKCPECGQPVE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 667 EVEQCQQLAEARHR------ELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRL 740
Cdd:PRK02224 463 GSPHVETIEEDRERveeleaELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 741 QAQVVDLQAKMRAALDDQDKVQSQlsmAEAVLREHKTLVQQLKEQNEALNR-AHVQELL----QCSEREGALQEERADEA 815
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEE---AEEAREEVAELNSKLAELKERIESlERIRTLLaaiaDAEDEIERLREKREALA 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 816 Q---QREEELRALQEELSQAKCSSEEAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAA 892
Cdd:PRK02224 620 ElndERRERLAEKRERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697
|
650 660
....*....|....*....|....*.
gi 1896085763 893 SReREGLERQVAGLQ---QEKESLQE 915
Cdd:PRK02224 698 ER-REALENRVEALEalyDEAEELES 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-1118 |
7.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 736 EVQRLQAQVVDLQAKM---RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnRAHVQELLQCsEREGALQEERA 812
Cdd:COG4717 72 ELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEAL-EAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 813 DEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALAcAVQELQDAKEAA 892
Cdd:COG4717 149 EELEERLEELRELEEEL-------EELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQ-RLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 893 SREREGLERQVAGLQQEKESLQEK------------------LKAAKAAAGSLP-----------GLQAQLAQAEQRAQS 943
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLIltiagvlflvlGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 944 LQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH--LAE 1021
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1022 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnRERNDQKMLADLDDLNRTKKYLEERLIELLRDKD 1101
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELA 456
|
410
....*....|....*..
gi 1896085763 1102 ALWQKSDALEFQQKLSA 1118
Cdd:COG4717 457 ELEAELEQLEEDGELAE 473
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
203-1095 |
8.44e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 203 ERMQQLdreNQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLE--LGAAE 280
Cdd:TIGR00606 189 ETLRQV---RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 281 KEEDYHTALRRLESMLQPLAQELEATRDSL----DKKNQHLASFPGwlAMAQQKADTASDTKGRQEPIpsdaAQEMQELG 356
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQ--RTVREKERELVDCQRELEKL----NKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 357 EKLQALERERTKVE---EVNRQQSAQLEQLVKELQLKEDAR-----ASLERLVKEMAPLQEE-LSGKGQEADQLWRRLQE 427
Cdd:TIGR00606 340 QEKTELLVEQGRLQlqaDRHQEHIRARDSLIQSLATRLELDgfergPFSERQIKNFHTLVIErQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 428 LLAHTsswEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSqqvgMLER 507
Cdd:TIGR00606 420 KERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS----KAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 508 LAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVG---RN 584
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 585 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR-KAKEAMKAQmaekeailqSKEGECQQ 663
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdKLFDVCGSQ---------DEESDLER 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 664 LREEVEQCQQ----------LAEARHRELRALESQC--------QQQTQLIEVLTAEKGQQGVGP----PTDNEARELAA 721
Cdd:TIGR00606 644 LKEEIEKSSKqramlagataVYSQFITQLTDENQSCcpvcqrvfQTEAELQEFISDLQSKLRLAPdklkSTESELKKKEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 722 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEA-------------VLREHKTLVQQLKEQNEA 788
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtimpeeesakVCLTDVTIMERFQMELKD 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 789 LNRAHVQELLQCSEREGALQ-EERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCAL 867
Cdd:TIGR00606 804 VERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 868 TVEKERVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQeklkaakaaagslpglqaqlaqaeQRAQSLQEA 947
Cdd:TIGR00606 884 QQFEEQLVE-LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI------------------------SSKETSNKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 948 AHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA-EEAVEKLKATQADMGE-KLSCTSNHLAEC--- 1022
Cdd:TIGR00606 939 AQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLmRQDIDTQKIQERwlq 1018
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1023 -QAAMLRKDKEGAALREDLERTQKEL-EKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1095
Cdd:TIGR00606 1019 dNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1122-1190 |
9.65e-07 |
|
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.
Pssm-ID: 277300 Cd Length: 76 Bit Score: 47.65 E-value: 9.65e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 1122 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHG------GKKERCCRACFqklSEGPGSPD 1190
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIkLNNSAeydpknGKWCRCCEKCF---TSRPGYND 76
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
642-893 |
1.13e-06 |
|
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: 52.46 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 642 AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAA 721
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 722 QLALSQAQLEVHQGEVQRL--QAQVVDLQAKMRAALDDQDKVQSQ--LSMAEAVLREHKTLVQQLKEQNEALNRAHvqel 797
Cdd:COG4942 91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALR---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 798 lqcseregALQEERADEAQQREEELRALQEELSQAKcsseeaqlehAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 877
Cdd:COG4942 167 --------AELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*.
gi 1896085763 878 LACAVQELQDAKEAAS 893
Cdd:COG4942 229 IARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
590-839 |
1.27e-06 |
|
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: 52.46 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 590 KLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQskegecqQLREEVE 669
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 670 QCQQLAEARHRELRALESQCQ---QQTQLIEVLTAEkgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQVVD 746
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYrlgRQPPLALLLSPE------------DFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 747 LQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvqellqcsEREGALQEERADEAQQREEELRALQ 826
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARL---------EKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 1896085763 827 EELSQAKCSSEEA 839
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
467-823 |
1.36e-06 |
|
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: 53.42 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 467 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpeLPVAGEKNEAlvpvnsSLQEAWGKPEEEQRG 546
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-------LPQANLLADE------TLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 547 LQEAQLddtkvqegsqeeELRQANRELEkELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 626
Cdd:COG3096 905 AQEAQA------------FIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFS 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 627 DQMEASLLAVRKA-KEAMKAQMAEKEAilqskegECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQ 705
Cdd:COG3096 972 YEDAVGLLGENSDlNEKLRARLEQAEE-------ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 706 QGVGPPTDNEAR------ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlreHKTLV 779
Cdd:COG3096 1045 LGVQADAEAEERarirrdELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA----GWCAV 1120
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 780 QQLKEQNEALNRAHVQELLQCSERE---------GALQEERADeaqqrEEELR 823
Cdd:COG3096 1121 LRLARDNDVERRLHRRELAYLSADElrsmsdkalGALRLAVAD-----NEHLR 1168
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
466-692 |
1.69e-06 |
|
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: 52.07 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 466 QLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagekneALVPVNSSLQEAwgkpeEEQR 545
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------------RIAALARRIRAL-----EQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 546 GLQEAQLDDTKVQEGSQEEELRQANRELEKELQNV--VGRNQLLEG------------KLQALQADYQALQQRESAIQGS 611
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllspedfldavrRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 612 LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ 691
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1896085763 692 Q 692
Cdd:COG4942 239 A 239
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1126-1179 |
1.83e-06 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.
Pssm-ID: 277258 [Multi-domain] Cd Length: 70 Bit Score: 46.93 E-value: 1.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 1126 TEANHCLDCKREFSW----M-------VRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACF 1179
Cdd:cd15718 4 AESDNCQKCSRPFFWnfkqMwekktlgVRQHHCRKCGKAVCDKCSSNRsTIPVMGFEFPvRVCNECY 70
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
563-917 |
2.21e-06 |
|
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: 51.82 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 563 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 642
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 643 MKAqmaEKEAILQSKEGECQQLREEVEQCQQLAEA---RHRELRALESQCQQQT-QLIEVLTAEKGQQGVGPPTDNEARE 718
Cdd:pfam07888 113 LSE---EKDALLAQRAAHEARIRELEEDIKTLTQRvleRETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 719 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------AKMRAALDDQDKVQSQLSM----AEAVLREHKTLVQQLKE 784
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttahrkeAENEALLEELRSLQERLNAserkVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 785 QNEALNRAHVQEL---LQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 861
Cdd:pfam07888 270 TQAELHQARLQAAqltLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 862 IQV-CALTVEKERVEEalacaVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 917
Cdd:pfam07888 350 REKdCNRVQLSESRRE-----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
765-1111 |
2.99e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 765 LSMAEAVLREHKTLVQQ---LKEQNEALNRAhvqellqcseregalQEERADEAQQREEELRALQEELSQAKCSSEEAQL 841
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQiseLKKQNNQLKDN---------------IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 842 EHAELQEQLHRANTDTAELGIQVCALTVE-----KERVEEALACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEK 916
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEK----KLEEIQNQISQNNKIISQLNEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 917 LKAAKAAAGSLPG----LQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQ 992
Cdd:TIGR04523 344 ISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 993 AAEEAVEKLKATQADMGEKLSCTSNhlaecqaamlrKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERND 1072
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTN-----------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350
....*....|....*....|....*....|....*....
gi 1896085763 1073 QKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE 1111
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
355-758 |
3.25e-06 |
|
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: 51.43 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 355 LGEKLQALERERTkveEVNRQQSAQLEQLVKELQLKEDARASLERLVKEM----APLQEELSGKGQEADQLWRRLQELLA 430
Cdd:pfam07888 32 LQNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELesrvAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 431 HTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlag 510
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE---- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 511 ppgpelpvageknEALVPVNSSLQEAwgKPEEEQRGLQEAQLDDTKVQegsqeeelrqanrelekeLQNVVGRNQLLEGK 590
Cdd:pfam07888 185 -------------EELRSLSKEFQEL--RNSLAQRDTQVLQLQDTITT------------------LTQKLTTAHRKEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 591 LQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAekEAILQSKEGECQQLREEvEQ 670
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA--DASLALREGRARWAQER-ET 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 671 CQQLAEARH-------RELRALESQCQQQTQLIEVLTAEKGQQ-----GVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 738
Cdd:pfam07888 309 LQQSAEADKdrieklsAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQ 388
|
410 420
....*....|....*....|
gi 1896085763 739 RLQAQVVDLQAKMRAALDDQ 758
Cdd:pfam07888 389 ELLEYIRQLEQRLETVADAK 408
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
600-1121 |
3.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 600 ALQQRESAIQGSLASLEAEQASIRH-LG-DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEgECQQLREEVEQcqQLAEA 677
Cdd:PRK03918 129 AIYIRQGEIDAILESDESREKVVRQiLGlDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEK--ELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 678 RhRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ---AKMRAA 754
Cdd:PRK03918 206 L-REINEISSELPELREELEKLEKEV----------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEeriEELKKE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 755 LDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKC 834
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE--IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 835 SSEEAQLEHAELQE---QLHRANTDTAELGIQvcaltvEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKE 911
Cdd:PRK03918 353 RLEELEERHELYEEakaKKEELERLKKRLTGL------TPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 912 SLQEKLKAAKAAAGSLPGLQAQLAqaEQRAQSLQEAAHQELNtlkfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQgRQL 991
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGRELT--EEHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKE-SEL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 992 QAAEEAVEKLKATQadmgEKLSCTSnhlaecqaamlrkdkegaalREDLERTQKELEKattkIQEYYNKLCQEVTNRERN 1071
Cdd:PRK03918 496 IKLKELAEQLKELE----EKLKKYN--------------------LEELEKKAEEYEK----LKEKLIKLKGEIKSLKKE 547
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1072 dqkmLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1121
Cdd:PRK03918 548 ----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
633-1113 |
4.37e-06 |
|
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: 51.51 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 633 LLAVRKAKEAMKAQMAEKEAILQSKEGecqqlREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgppt 712
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEKKELLMNLFP-----LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDT------ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 713 dneARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRA 792
Cdd:TIGR00618 217 ---YHERKQVLEKELKHLREALQQTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 793 --------HVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQv 864
Cdd:TIGR00618 290 rkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 865 caltvEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLaQAEQRAQSL 944
Cdd:TIGR00618 369 -----EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 945 QEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC-- 1022
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdn 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1023 ----QAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK---LCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1095
Cdd:TIGR00618 523 pgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....*...
gi 1896085763 1096 LLRDKDALWQKSDALEFQ 1113
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRK 620
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
531-1063 |
4.68e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 531 SSLQEAWGKPEEEQRGLQEAQLDDTKV----QEGSQE--------------------------EELRQANRELEKELQNV 580
Cdd:pfam05483 106 NKLQENRKIIEAQRKAIQELQFENEKVslklEEEIQEnkdlikennatrhlcnllketcarsaEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 581 VGRNQLLEGKLQALQadyQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEA-------I 653
Cdd:pfam05483 186 MDLNNNIEKMILAFE---ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENkmkdltfL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 654 LQSKEGECQQLREEV----EQCQQLAEARHRELRALES-QCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQA 728
Cdd:pfam05483 263 LEESRDKANQLEEKTklqdENLKELIEKKDHLTKELEDiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 729 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE--QNEALNRAHVQELLqcSEREGA 806
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfkNNKEVELEELKKIL--AEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 807 LQEERADEA----------------QQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVE 870
Cdd:pfam05483 421 LDEKKQFEKiaeelkgkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 871 KERVEEALACAVQELQDAKE---AASREREGLERQVAGLQQEKESLQEKLKAAKAA-AGSLPGLQAQLAQAEQRAQSLQE 946
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 947 AAHQELNTLKF------QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL-SCTSNHL 1019
Cdd:pfam05483 581 EVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFeEIIDNYQ 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1896085763 1020 AECQAAMLRKDKegaaLREDLERTQKELEKAtTKIQEYYNKLCQ 1063
Cdd:pfam05483 661 KEIEDKKISEEK----LLEEVEKAKAIADEA-VKLQKEIDKRCQ 699
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
715-847 |
5.18e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 50.43 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 715 EARELAAQLALSQAQLEVHQGEVQRLQAQVvDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHV 794
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEAEL-GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARA 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 795 QELLQCSEREGALQEERADEAQQRE-EELRALQEELSQAkcsseEAQLEHAELQ 847
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQAGLREeEELAAAQAQVAQA-----EAALAQAELN 204
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
178-631 |
5.94e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 178 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAE--LQKQWE 255
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-RDDLLAEAGLDDADAEavEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 256 VTQATQNTVKELQTCLQGLEL------GAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQ 329
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAhneeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 330 KADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE--------QLVKE---LQLKEDARASLE 398
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 399 RLVKEMAPLQEELSGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQ-- 476
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEkr 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 477 ------------VSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGpPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQ 544
Cdd:PRK02224 558 eaaaeaeeeaeeAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKRERK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 545 RGLqEAQLDDTKVqegsqeEELRQANRELEKELQNVvgrnqllEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 624
Cdd:PRK02224 637 REL-EAEFDEARI------EEAREDKERAEEYLEQV-------EEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
....*..
gi 1896085763 625 LGDQMEA 631
Cdd:PRK02224 703 LENRVEA 709
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
714-951 |
7.25e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 714 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREH----------KTLVQQL- 782
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDVLl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 783 --KEQNEALNRAHVQELLQcseregALQEERADEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANTDTAEL 860
Cdd:COG3883 110 gsESFSDFLDRLSALSKIA------DADADLLEELKADKAELEAKKAELEAKL---AELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 861 GIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR 940
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
250
....*....|.
gi 1896085763 941 AQSLQEAAHQE 951
Cdd:COG3883 261 SAGAAGAAAGA 271
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
188-685 |
9.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 188 RLELDQLEVREKQLRERMQQLDrENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKEL 267
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 268 QTCLQGLElgaaEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLaSFPGWLAMaqqkadtasdtkgrqepipSD 347
Cdd:COG4717 145 PERLEELE----ERLEELRELEEELEE----LEAELAELQEELEELLEQL-SLATEEEL-------------------QD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 348 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARaslerlvkemaplqeelsgKGQEADQLWRRLQE 427
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-------------------RLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 428 LLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmler 507
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 508 lagppGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLddtkvqEGSQEEELRQANRELEKELQNVVGRNQLL 587
Cdd:COG4717 329 -----GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL------EQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 588 EGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQ--SKEGECQQLR 665
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELAELEAELEqlEEDGELAELL 475
|
490 500
....*....|....*....|
gi 1896085763 666 EEVEQCQQLAEARHRELRAL 685
Cdd:COG4717 476 QELEELKAELRELAEEWAAL 495
|
|
| RUN_RUFY1 |
cd17694 |
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
32-122 |
1.14e-05 |
|
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homolog of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.
Pssm-ID: 439056 Cd Length: 156 Bit Score: 46.82 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17694 24 GRTLDSDYPPLQQFFVVLEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLA 103
|
90
....*....|.
gi 1896085763 112 LVHQRLADTLQ 122
Cdd:cd17694 104 LMQKKLADYLK 114
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-404 |
1.26e-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: 50.06 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 178 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVT 257
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 258 QAT-----------QNTVKELQTCLQGLELGAAEKEEDYHTALRRLESM---LQPLAQELEATRDSLDKKNQHLASFPGW 323
Cdd:TIGR02168 851 SEDieslaaeieelEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 324 LAMAQQKADT--------ASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVN-------RQQSAQLEQLVKELQ 388
Cdd:TIGR02168 931 LEGLEVRIDNlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyEELKERYDFLTAQKE 1010
|
250
....*....|....*.
gi 1896085763 389 LKEDARASLERLVKEM 404
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEI 1026
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1131-1182 |
1.29e-05 |
|
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.
Pssm-ID: 277262 [Multi-domain] Cd Length: 62 Bit Score: 44.03 E-value: 1.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 1131 CLDCKREFS-WMVRRHHCRICGRIFCYYCCNNYVLSKHGG------KKE--RCCRACFQKL 1182
Cdd:cd15723 2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVPRSVMGatapaaQREtvFVCSGCNDKL 62
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
561-1111 |
1.66e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 561 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQ---QRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR 637
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 638 KAKEAMKAQMAEkeaiLQSKEGECQQLREEVEqcqqlaeaRHRELRALESQCQQQTQLIEVLTAEkgqqgvgppTDNEAR 717
Cdd:PRK03918 266 ERIEELKKEIEE----LEEKVKELKELKEKAE--------EYIKLSEFYEEYLDELREIEKRLSR---------LEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 718 ELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMrAALDDQDKVQSQLSMAEAVLREHKTlvqqlKEQNEALNRAhVQEL 797
Cdd:PRK03918 325 GIEERIK----ELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKK-----RLTGLTPEKL-EKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 798 LQCSEREGALQEE------RADEAQQREEELRALQEELSQAK-----CSSEEAQLEHAELQE----QLHRANTDTAELGI 862
Cdd:PRK03918 394 EELEKAKEEIEEEiskitaRIGELKKEIKELKKAIEELKKAKgkcpvCGRELTEEHRKELLEeytaELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 863 QVCALTVEKERVEEALAcAVQELQDAKEAASREREgLERQVAGLQQEKesLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQ 942
Cdd:PRK03918 474 KERKLRKELRELEKVLK-KESELIKLKELAEQLKE-LEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 943 SLQEaahqelntlkfqLSAEIMDYQSRLKNAGEECKSLRGQLEEQGrqLQAAEEAVEKLKATQADMGEKLScTSNHLAEC 1022
Cdd:PRK03918 550 KLEE------------LKKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKELEPFYNEYLE-LKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1023 QAAMLRKDKEGAAL---REDLERTQKELEKATTKI--------QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE 1091
Cdd:PRK03918 615 EREEKELKKLEEELdkaFEELAETEKRLEELRKELeelekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580
....*....|....*....|
gi 1896085763 1092 RLIELLRDKDALWQKSDALE 1111
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELE 714
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
562-1052 |
1.71e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 562 QEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAiQGSLASLEAEQ--ASIRHLGD---QMEASLLAV 636
Cdd:PRK10246 231 EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-QPQLAALSLAQpaRQLRPHWEriqEQSAALAHT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 637 RKAKEAMKAQMAEKEA----ILQSKEGECQQLREEVEQCQQ-LAEAR-----HREL---RALESQC----QQQTQLIEVL 699
Cdd:PRK10246 310 RQQIEEVNTRLQSTMAlrarIRHHAAKQSAELQAQQQSLNTwLAEHDrfrqwNNELagwRAQFSQQtsdrEQLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 700 TAEKGQQGVGPPT--DNEARELAAQLALSQAQLEVHQgEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKt 777
Cdd:PRK10246 390 THAEQKLNALPAItlTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMR- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 778 lvQQLKEQNEALNRahVQELLQCSEREGALQEERA---------------------------DEAQQR----EEELRALQ 826
Cdd:PRK10246 468 --QRYKEKTQQLAD--VKTICEQEARIKDLEAQRAqlqagqpcplcgstshpaveayqalepGVNQSRldalEKEVKKLG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 827 EELSQAKcsseeAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAK----EAASRERE----- 897
Cdd:PRK10246 544 EEGAALR-----GQLD--ALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldAQEEHERQlrlls 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 898 ----------GLERQVAGLQQEKESLQEKLKAAKAAAG-SLPGLQAQ---LAQAEQRAQSLQeAAHQELNTLKFQLSA-- 961
Cdd:PRK10246 617 qrhelqgqiaAHNQQIIQYQQQIEQRQQQLLTALAGYAlTLPQEDEEaswLATRQQEAQSWQ-QRQNELTALQNRIQQlt 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 962 ---------EIMDYQS------RLKNAGEECKSLRGQLEEQGRQlqaaeEAVEKLKATQADMGEKLSCTSNHLAECQA-- 1024
Cdd:PRK10246 696 plletlpqsDDLPHSEetvaldNWRQVHEQCLSLHSQLQTLQQQ-----DVLEAQRLQKAQAQFDTALQASVFDDQQAfl 770
|
570 580
....*....|....*....|....*...
gi 1896085763 1025 AMLRKDKEGAALREDLERTQKELEKATT 1052
Cdd:PRK10246 771 AALLDEETLTQLEQLKQNLENQRQQAQT 798
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
650-915 |
2.73e-05 |
|
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: 48.35 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 650 KEAILQSKEGECQQLREEVEQCQQLA------------------EARHRELRA----LESQCQQQTQLIEVLTAE-KGQQ 706
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAAnrqrekekerykrdreqwERQRRELESrvaeLKEELRQSREKHEELEEKyKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 707 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 786
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 787 EALNRAHVQELLQCSEREGALQE---------ERADEAQQRE-------EELRALQEELSQAKCSSEEAQLEHAEL---- 846
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQlqdtittltQKLTTAHRKEaeneallEELRSLQERLNASERKVEGLGEELSSMaaqr 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 847 ---QEQLHRANTDTAELGIQVCALTVEkerVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQE 915
Cdd:pfam07888 268 drtQAELHQARLQAAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
729-1093 |
3.86e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 729 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTL-------VQQLKEQNEALNRAHVQELLQCS 801
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKikelekqLNQLKSEISDLNNQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 802 EREGALQEERADEAQ----QREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 877
Cdd:TIGR04523 313 KSELKNQEKKLEEIQnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 878 LACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQ------E 951
Cdd:TIGR04523 393 INDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIER----------LKETIIKNNSEIKDLTNQDSVkeliikN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 952 LNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDK 1031
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 1032 EGAALREDLER-----TQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 1093
Cdd:TIGR04523 539 KISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| RUN_RUFY3 |
cd17696 |
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ... |
32-137 |
3.86e-05 |
|
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. This model represents the RUN domain of RUFY3.
Pssm-ID: 439058 Cd Length: 156 Bit Score: 45.37 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17696 24 GRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLA 103
|
90 100
....*....|....*....|....*.
gi 1896085763 112 LVHQRLADtlqqcFMNTKVTRRTLTT 137
Cdd:cd17696 104 LMQKKLSE-----YMKALINRKDLLS 124
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
348-994 |
4.08e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.26 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 348 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQE--------ELSGKGQEAD 419
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpqlaalSLAQPARQLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 420 QLWRRLQEllaHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEE------------- 486
Cdd:PRK10246 294 PHWERIQE---QSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnelagwra 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 487 QKKQLIQDKDHLSQQVGML-----ERLAGPPGPELPVAGEKNEALVPVN---------SSLQEAWGKPEEEQRGLQEA-- 550
Cdd:PRK10246 371 QFSQQTSDREQLRQWQQQLthaeqKLNALPAITLTLTADEVAAALAQHAeqrplrqrlVALHGQIVPQQKRLAQLQVAiq 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 551 QLDDTKVQEGSQEEELRQANRELEKELQNVVG------RNQLLEGKLQALQA----------------DYQALQQreSAI 608
Cdd:PRK10246 451 NVTQEQTQRNAALNEMRQRYKEKTQQLADVKTiceqeaRIKDLEAQRAQLQAgqpcplcgstshpaveAYQALEP--GVN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 609 QGSLASLEAEQASIRHLGdqmeaslLAVRKAKEAMKAQmaekeaiLQSKEGECQQLREEVeqcQQLAEARHRELRALESQ 688
Cdd:PRK10246 529 QSRLDALEKEVKKLGEEG-------AALRGQLDALTKQ-------LQRDESEAQSLRQEE---QALTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 689 CQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALsQAQLEVHQGEVQRLQAQVVDLQAKMRAALD-------DQDKV 761
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHE-------RQLRLLSQRHEL-QGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltlpQEDEE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 762 QSQLSMAEAvlrEHKTLVQQLKEQNEALNR-AHVQELLQCSEREGALQEERADEAQqreEELRALQEElsqakCSSEEAQ 840
Cdd:PRK10246 664 ASWLATRQQ---EAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVAL---DNWRQVHEQ-----CLSLHSQ 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 841 LEHAELQEQLHRANTDTAElgiqvcaltvekERVEEALACAVQELQDAKEAASREREGLERqvagLQQEKESLQEKLKAA 920
Cdd:PRK10246 733 LQTLQQQDVLEAQRLQKAQ------------AQFDTALQASVFDDQQAFLAALLDEETLTQ----LEQLKQNLENQRQQA 796
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 921 KAaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQL--EEQGRQLQAA 994
Cdd:PRK10246 797 QT-------LVTQTAQALAQHQQHRPDGLDLTVTVE-QIQQELAQLAQQLRENTTRQGEIRQQLkqDADNRQQQQA 864
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
563-943 |
4.08e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 563 EEELRQanrELeKELQNVVGRNQLleGKLQALQADYQALQQResaiQGSLASLEAEQASI-------RHLGDQMEASLLA 635
Cdd:PRK10929 25 EKQITQ---EL-EQAKAAKTPAQA--EIVEALQSALNWLEER----KGSLERAKQYQQVIdnfpklsAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 636 VRKAKEAMKAQMAEKEaILQSKegecQQLREEVEQCQQLAEaRHRELRALESQC-QQQTQLIEVLT-AEKGQQGVGPPTD 713
Cdd:PRK10929 95 PRSVPPNMSTDALEQE-ILQVS----SQLLEKSRQAQQEQD-RAREISDSLSQLpQQQTEARRQLNeIERRLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 714 nearelaaqlALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAH 793
Cdd:PRK10929 169 ----------PLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAK---KRSQQLDAYLQALRNQLNSQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 794 VQELLQCSEREGALQEERADEAQQREEELRaLQEELSQAkcSSEEAQlEHAELQEQLHRANTDTaelgIQV-CALTVEKE 872
Cdd:PRK10929 236 QREAERALESTELLAEQSGDLPKSIVAQFK-INRELSQA--LNQQAQ-RMDLIASQQRQAASQT----LQVrQALNTLRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 873 RVE---------EALACAVQELQDAKEAASREREGLERQVAGLQQEK--ESLQEKLKAAKAAAGSLPGLQAQLAQAEQRA 941
Cdd:PRK10929 308 QSQwlgvsnalgEALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDllNKQPQLRQIRQADGQPLTAEQNRILDAQLRT 387
|
..
gi 1896085763 942 QS 943
Cdd:PRK10929 388 QR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
192-430 |
4.18e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 192 DQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQterergrtaaednvrltclvaELQKQWEVTQATQNTVKELQTCL 271
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---------------------QLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 272 QGLELGAAEKEEDYHTALRRLESMLQPLAQEL-EATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIpSDAAQ 350
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 351 EMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLErlvKEMAPLQEELSGKGQEADQLWRRLQELLA 430
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEA 234
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
638-1119 |
4.18e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 638 KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ----CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptd 713
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAqrkaIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLC------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 714 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQdKVQSQLSMAEA--VLREHKTLVQQLKE--QNEAL 789
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-RVQAENARLEMhfKLKEDHEKIQHLEEeyKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 790 NRAHVQELL--QCSEREGALQ------EERADEAQQREEELRALQEELSQA--KCSSEEAQLEHAELQEQLHRANTDTAE 859
Cdd:pfam05483 237 DKEKQVSLLliQITEKENKMKdltfllEESRDKANQLEEKTKLQDENLKELieKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 860 LGIQV-----CALTVEKErveealaCAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQ 933
Cdd:pfam05483 317 EDLQIatktiCQLTEEKE-------AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 934 LAQAEQRAQsLQEAAHQELNTLKFQLSAE--IMDYQSRLKNAGEEcksLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1011
Cdd:pfam05483 390 SSELEEMTK-FKNNKEVELEELKKILAEDekLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1012 LSCTSNHLAECQAAMLR---KDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKY 1088
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
490 500 510
....*....|....*....|....*....|.
gi 1896085763 1089 LEErliELLRDKDALWQKSDALEFQQKLSAE 1119
Cdd:pfam05483 546 LRD---ELESVREEFIQKGDEVKCKLDKSEE 573
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
347-682 |
4.38e-05 |
|
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: 48.41 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 347 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLkedarasLERLVKEMAPLQEE-LSGKGQEADQLWRRL 425
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-------LNKLLPQANLLADEtLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 426 QELLAHTSSweeelaelrrekkqqqeekelLEQEVRSLTRQLQFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQV 502
Cdd:COG3096 906 QEAQAFIQQ---------------------HGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVV 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 503 GMLERLagppgpelpvAGEKNEALVPVNSSLQEAWgkpeeeqrglqEAQLDDTKVQEGSQEEELRQANRELEKELQnvvg 582
Cdd:COG3096 965 QRRPHF----------SYEDAVGLLGENSDLNEKL-----------RARLEQAEEARREAREQLRQAQAQYSQYNQ---- 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 583 RNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGEC- 661
Cdd:COG3096 1020 VLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRR--DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLr 1097
|
330 340 350
....*....|....*....|....*....|..
gi 1896085763 662 ------QQLREEVEQ-----CQQLAEARHREL 682
Cdd:COG3096 1098 kaerdyKQEREQVVQakagwCAVLRLARDNDV 1129
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
542-852 |
4.61e-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: 48.20 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 542 EEQRGLQEAQlddtkvqEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGS-LASLEAEQA 620
Cdd:pfam17380 313 ERRRKLEEAE-------KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISrMRELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 621 SIRHLGDQMEASLLAVRKakeaMKAQMAEKEAILQSKEGECQQLREEVEqcqqlaEARHRELRALESQCQQQTQLIEVLT 700
Cdd:pfam17380 386 ERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMEQIRAEQE------EARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 701 AEKgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQsqlsMAEAVLREHKTLVQ 780
Cdd:pfam17380 456 QER-QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK----LLEKEMEERQKAIY 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 781 QLKEQNEAlnrahvqellqcseregalQEERadEAQQREEELRALQEELSQAkcSSEEAQLEHAELQEQLHR 852
Cdd:pfam17380 531 EEERRREA-------------------EEER--RKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMR 579
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
565-700 |
4.69e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.11 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 565 ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQ--------------ASIRHLGDQME 630
Cdd:pfam15905 160 ELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKieekseteklleyiTELSCVSEQVE 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 631 ASLLAVRKAKEAMKAQMAE----KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLT 700
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEieslKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELK 313
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
464-798 |
5.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 464 TRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAG------EKNEALVPVNSS----- 532
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiaELEAELERLDASsddla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 533 -LQEAWGKPEEEQRGLQEaQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLE-GKLQALQADYQAL--QQRESAI 608
Cdd:COG4913 689 aLEEQLEELEAELEELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAAlgDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 609 QGSL-ASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEveqcqQLAEARHRELRALES 687
Cdd:COG4913 768 RENLeERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED-----GLPEYEERFKELLNE 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 688 QCQQ-QTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkMRAALDDQDKVQSQLS 766
Cdd:COG4913 843 NSIEfVADLLSKLRRAI----------REIKERIDPLNDSLKRIPFGPGRYLRLEARPRPDPE-VREFRQELRAVTSGAS 911
|
330 340 350
....*....|....*....|....*....|....*..
gi 1896085763 767 MAEAVLREH-----KTLVQQLKEQNEALNRAHVQELL 798
Cdd:COG4913 912 LFDEELSEArfaalKRLIERLRSEEEESDRRWRARVL 948
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
592-1048 |
5.51e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 592 QALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 671
Cdd:COG3899 770 RALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREA 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 672 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 751
Cdd:COG3899 850 LELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAA 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 752 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 831
Cdd:COG3899 930 ALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAA 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 832 AkCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 911
Cdd:COG3899 1010 A-AAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAAL 1088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 912 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 991
Cdd:COG3899 1089 AAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAA 1168
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 992 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1048
Cdd:COG3899 1169 LALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
198-1000 |
6.75e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 198 EKQLRERMQQLDRENQElRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEvtQATQNTVKELQTCLQGLELG 277
Cdd:pfam01576 270 EAQISELQEDLESERAA-RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 278 AAEKEEDYHTALRRLESMLQPLA---QELEATRDSLDKKNQHLasfpgwlamaQQKADTASDTKGRQEPIPSDAAQEMQE 354
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKrnkANLEKAKQALESENAEL----------QAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 355 LGEKLQALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKEMAPLQEELsgkgQEADQLwrrLQELLAHTSS 434
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQL----QDTQEL---LQEETRQKLN 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 435 WEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLA-------QVSQHVSDLEEQKKQLIQDKDHLSQQvgMLER 507
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmkkkleEDAGTLEALEEGKKRLQRELEALTQQ--LEEK 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 508 LAGPPGPELP---VAGEKNEALVPVNSSLQEAwGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELqnvvgRN 584
Cdd:pfam01576 565 AAAYDKLEKTknrLQQELDDLLVDLDHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET-----RA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 585 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGecQQL 664
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED--AKL 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 665 REEVeqcqqlaearhrELRALESQCQQQTQLIEVLTAEKGQQGVgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQV 744
Cdd:pfam01576 717 RLEV------------NMQALKAQFERDLQARDEQGEEKRRQLV-----KQVRELEAELEDERKQRAQAVAAKKKLELDL 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 745 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKtlvqqlKEQNEAlnRAHVQELLQCSeregalqEERADEAQQREEELRA 824
Cdd:pfam01576 780 KELEAQIDAANKGREEAVKQLKKLQAQMKDLQ------RELEEA--RASRDEILAQS-------KESEKKLKNLEAELLQ 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 825 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcALTVEKERVEEALACAVQELQDAKEAAsrerEGLERQVA 904
Cdd:pfam01576 845 LQEDLAASERARRQAQQERDELADEIASGASGKS-------ALQDEKRRLEARIAQLEEELEEEQSNT----ELLNDRLR 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 905 GLQQEKESLQEKLKAAKAAAGSLPGLQAQLaqaEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEeckslrgQL 984
Cdd:pfam01576 914 KSTLQVEQLTTELAAERSTSQKSESARQQL---ERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEE-------QL 983
|
810
....*....|....*.
gi 1896085763 985 EEQGRQLQAAEEAVEK 1000
Cdd:pfam01576 984 EQESRERQAANKLVRR 999
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-757 |
7.89e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 193 QLEVREKQLRERMQQLDRENQELRAAVSQQGE-QLQTERERGRTAAEDNVRL-----TCLVAELQKQWEVTQATQNTVKE 266
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDahevaTSIREISCQQHTLTQHIHTLQQQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 267 LQTCLQGLELGAAEKEEdyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 346
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDI-----LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 347 DAAQEMQELGEKLQALER-----ERTKVEEVNRQQSAQLEQLVKELQLKEDARAS-----LERLVKEMAPLQEELSGKGQ 416
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLET 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 417 EADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQH------VSDLEEQKKQ 490
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAedmlacEQHALLRKLQ 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 491 LIQDKDHLSQQVGMLER-----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGkpeeEQRGLQEAQLDDTKVQEGSQEEE 565
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQelalkLTALHALQLTLTQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTYWKEM 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 566 LRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASirhlgdqmeasllaVRKAKEAMKA 645
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART--------------VLKARTEAHF 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 646 QMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQT---QLIEVLTAEKGQQGVgPPTDNEARELAAQ 722
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdEDILNLQCETLVQEE-EQFLSRLEEKSAT 843
|
570 580 590
....*....|....*....|....*....|....*
gi 1896085763 723 LALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDD 757
Cdd:TIGR00618 844 LGEITHQLL-KYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| RUN_RUFY2 |
cd17695 |
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
32-135 |
8.20e-05 |
|
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. This model represents the RUN domain of RUFY2.
Pssm-ID: 439057 Cd Length: 156 Bit Score: 44.58 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 32 GEPITDDSTSLHKFSYKLEYLLQFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYS 111
Cdd:cd17695 24 GRTLDSDYPPLQQFFVVMEHCLKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLA 103
|
90 100
....*....|....*....|....
gi 1896085763 112 LVHQRLADTLqQCFMntkvTRRTL 135
Cdd:cd17695 104 LMQKKLADYL-RCLI----IRRDL 122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
771-1111 |
9.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 771 VLREHKTL--VQQLKEQNEALNRAHvQELLQCSEREGALQ--EERADEAQQREEELRALQEELSQAKcsSEEAQLEHAEL 846
Cdd:COG4913 217 MLEEPDTFeaADALVEHFDDLERAH-EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALR--LWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 847 QEQLHRantdtaelgiqvcaLTVEKERVEEALAcavqELQDAKEAASREREGLERQVAGLQ-QEKESLQEKLKaakaaag 925
Cdd:COG4913 294 EAELEE--------------LRAELARLEAELE----RLEARLDALREELDELEAQIRGNGgDRLEQLEREIE------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 926 slpGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAEImdyqsrlknagEECKSLRGQLEEQGRQLQAAEEAVEKLKAtq 1005
Cdd:COG4913 349 ---RLERELEERERRRARLEAL----LAALGLPLPASA-----------EEFAALRAEAAALLEALEEELEALEEALA-- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1006 admgeklsctsnhlaecqaamlrkdkegaalreDLERTQKELEKATTKIQeyynklcQEVTNRERN----DQKMLADLDD 1081
Cdd:COG4913 409 ---------------------------------EAEAALRDLRRELRELE-------AEIASLERRksniPARLLALRDA 448
|
330 340 350
....*....|....*....|....*....|....*
gi 1896085763 1082 LNRTKKYLEERL---IELL--RDKDALWQksDALE 1111
Cdd:COG4913 449 LAEALGLDEAELpfvGELIevRPEEERWR--GAIE 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
561-1117 |
1.11e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 561 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQ---MEASLLAVR 637
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQiseLKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 638 KAKEAMKAQMAEKEAILQSKEGECQQLREE-------VEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKgQQGVGP 710
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 711 PTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaeavlREHKTLVQQLKEQNEALN 790
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-------EEKQNEIEKLKKENQSYK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 791 RAHVQELLQCSEREGALQEERaDEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELgiqvcaltve 870
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEK-------ELLEKEIERLKETIIKNNSEIKDL---------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 871 kERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQE---- 946
Cdd:TIGR04523 446 -TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKkiss 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 947 --AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKS--LRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC 1022
Cdd:TIGR04523 522 lkEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1023 QAAMLRKDKEGAALREDLERTQKELEKATT---KIQEYYNKLCQEVTNRE---RNDQKMLADLDDLNRTKKYLEERLIEL 1096
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEVKQIKetiKEIRNKWPEIIKKIKESKTKIDDIIEL 681
|
570 580
....*....|....*....|.
gi 1896085763 1097 LRDkdalWQKSDALEFQQKLS 1117
Cdd:TIGR04523 682 MKD----WLKELSLHYKKYIT 698
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
650-917 |
1.21e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.21 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 650 KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQLALSQAQ 729
Cdd:pfam15742 4 GEKLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKA------ELKQAQQKLLDSTKM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 730 LEVHQGEVQRLQAQVVDLQAKMraaLDDQDKVQSQLSMAEAVLREHKTLVQQLK---EQNEALNRAHVQELLQCSEREGA 806
Cdd:pfam15742 78 CSSLTAEWKHCQQKIRELELEV---LKQAQSIKSQNSLQEKLAQEKSRVADAEEkilELQQKLEHAHKVCLTDTCILEKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 807 LQEERADEAQQREEELRA-LQEELSQAKCSSEEAQlehaELQEQLhRANTDTAELGIQVCALTVEKERVEEALACAVQEL 885
Cdd:pfam15742 155 QLEERIKEASENEAKLKQqYQEEQQKRKLLDQNVN----ELQQQV-RSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENE 229
|
250 260 270
....*....|....*....|....*....|..
gi 1896085763 886 QDAKEAASREREGLERQVAGLQQEKESLQEKL 917
Cdd:pfam15742 230 KRKSDEHLKSNQELSEKLSSLQQEKEALQEEL 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
188-757 |
1.46e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 188 RLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaednvrltclVAELQKQWEvtQATQNTVKEL 267
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE--------------LDELEAQIR--GNGGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 268 QTCLQGLELGAAEKE---EDYHTALRRLESMLQPLAQELEATRDSLDkknQHLASFPGWLAMAQQKADTASDTKgrqepi 344
Cdd:COG4913 344 EREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAAL------ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 345 pSDAAQEMQELGEKLQALERERTKVEEvnRQQSAqLEQLVKELQLKEDaraslerlvkEMAPLQEELSGKGQEADqlWRR 424
Cdd:COG4913 415 -RDLRRELRELEAEIASLERRKSNIPA--RLLAL-RDALAEALGLDEA----------ELPFVGELIEVRPEEER--WRG 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 425 LQELLAHTSSweeelaelrrekkqqqeekelleqevRSLtrqlqfL--ETQLAQVSQHVSDLeeqkkqliqdkdHLSQQV 502
Cdd:COG4913 479 AIERVLGGFA--------------------------LTL------LvpPEHYAAALRWVNRL------------HLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 503 gMLERLAGPPGPELPVAGEKNE--ALVPVNSSLQEAWGKPEEEQRGL-----QEAQLDDTK---VQEG--SQEEELRQAN 570
Cdd:COG4913 515 -VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLEAELGRRFDyvcvdSPEELRRHPraiTRAGqvKGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 571 RELEKELQNVVGRN-----QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgDQMEASLLAVRKAKEAMKA 645
Cdd:COG4913 594 DRRRIRSRYVLGFDnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 646 QMAEKEAILQSKeGECQQLREEVEQCQQLAEARHRELRALESQC----QQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 721
Cdd:COG4913 673 LEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
570 580 590
....*....|....*....|....*....|....*..
gi 1896085763 722 QLALSQAQLEVHQGEVQR-LQAQVVDLQAKMRAALDD 757
Cdd:COG4913 752 EERFAAALGDAVERELREnLEERIDALRARLNRAEEE 788
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
808-1008 |
1.85e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 808 QEERADEAQQReeeLRALQEELSQAKcsseeAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcavqELQD 887
Cdd:COG3206 166 LELRREEARKA---LEFLEEQLPELR-----KELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLA----EARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 888 AKEAASREREGLERQVAGLQQEKESLQEklkaakaaAGSLPGLQAQLAQAEQRAQSLQE----------AAHQELNTLKF 957
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 958 QLSAEIMDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM 1008
Cdd:COG3206 306 QLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
548-830 |
2.01e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 548 QEAQLDDTKVQEGSQEEELRQANRELE--KELQNVVGRNQL-------LEGKLQALQADYQALQQRESAIQGSLASLEAe 618
Cdd:PRK11281 78 QKEETEQLKQQLAQAPAKLRQAQAELEalKDDNDEETRETLstlslrqLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 619 qASIRhlgdqmeasllaVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVeqcQQLAEArhrELRALESQCQQQTQLIEV 698
Cdd:PRK11281 157 -QPER------------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ---RVLLQA---EQALLNAQNDLQRKSLEG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 699 LTaekgqqgvgpptdnearelaaQL-ALSQAQLEVHQGEVQRLQAQVVDLQakmrAALDDQDKVQSQLSMAEAVLREHKT 777
Cdd:PRK11281 218 NT---------------------QLqDLLQKQRDYLTARIQRLEHQLQLLQ----EAINSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 778 LVQQ--LKEQNEALNRAHVQELLQCSEREGAL--QEERA----DEAQQREeelRALQEELS 830
Cdd:PRK11281 273 RIQAnpLVAQELEINLQLSQRLLKATEKLNTLtqQNLRVknwlDRLTQSE---RNIKEQIS 330
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
328-774 |
2.06e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 328 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLV------ 401
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 402 KEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRRE----KKQQQEEKELLEQEVRSLTRQLQFLETQLAQV 477
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELqeelEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 478 SQHVSDLEEQKKQLIQDKDHLSQQ-------------------VGMLERLAGPPGPELPVAGEKNEALVPVNS--SLQEA 536
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEleaaaleerlkearlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 537 WGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQgsLASLE 616
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 617 AEQASIRHLGDqmeasllavrkakeamkaqmAEKEAilqskegecqQLREEVEQCQQLAEARhRELRALESQCQQQTQLI 696
Cdd:COG4717 370 QEIAALLAEAG--------------------VEDEE----------ELRAALEQAEEYQELK-EELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 697 EVLTAekgqqgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQ--DKVQSQLSMAEAVLRE 774
Cdd:COG4717 419 EELLE-----------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
225-878 |
2.62e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 225 QLQTERERgrtAAEDNVRLTCLVAELQKQWEVTQATQNT----VKELQTCLQGLELGAAEKEED---------YHTALRR 291
Cdd:pfam10174 120 RLQSEHER---QAKELFLLRKTLEEMELRIETQKQTLGArdesIKKLLEMLQSKGLPKKSGEEDwertrriaeAEMQLGH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 292 LESMLQPLAQELEATRDSLDKKNQhlasfpgwlamaqqkadtasdtkGRQEPIPSDAAQEMQELGE-KLQALERERTKVE 370
Cdd:pfam10174 197 LEVLLDQKEKENIHLREELHRRNQ-----------------------LQPDPAKTKALQTVIEMKDtKISSLERNIRDLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 371 -EVNRQQSAQL---EQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREK 446
Cdd:pfam10174 254 dEVQMLKTNGLlhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 447 KQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpELPVAGEKNEAL 526
Cdd:pfam10174 334 TAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 527 VPVNSSLQEAWGKPEEEQRGLQ--------------EAQLDDTKVQEGSQEEELRQaNRELEKELQNVVGRNQLLEGKLQ 592
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQtdssntdtalttleEALSEKERIIERLKEQRERE-DRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 593 ALQADYQA-------LQQRESAIQGS-------LASLEAEQASIRHLGDQMEASLLAVRKAKEA--MKAQMAEKeaiLQS 656
Cdd:pfam10174 486 ALQPELTEkesslidLKEHASSLASSglkkdskLKSLEIAVEQKKEECSKLENQLKKAHNAEEAvrTNPEINDR---IRL 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 657 KEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTdnearelaaqlalSQAQLEVHQGE 736
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNK-------------KVANIKHGQQE 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 737 VQRLQAQVVDLQakmRAALDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALnrAHVQELLQcsEREGALQEERADEAQ 816
Cdd:pfam10174 630 MKKKGAQLLEEA---RRREDNLADNSQQLQLEELMGALEKTR-QELDATKARL--SSTQQSLA--EKDGHLTNLRAERRK 701
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 817 QREEELRALQEELsQAKCSSEEAQLEHAELQEQLHRANTDtaelgiQVCALTVEKERVEEAL 878
Cdd:pfam10174 702 QLEEILEMKQEAL-LAAISEKDANIALLELSSSKKKKTQE------EVMALKREKDRLVHQL 756
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
592-856 |
2.75e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 592 QALQADYQALQQRESaiqgslasLEAEQASIRHLGDQMEASLlavrKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 671
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 672 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGE----VQRLQ---AQV 744
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQ-------NDLAEYNSQLVSLQTQPERAQAAlyanSQRLQqirNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 745 VDLQAKMRAALDDQ-DKVQSQLSMAEAVLRehktLVQQLKEQNEALnrahvQELLQcSEREgalqeERADEAQQREEELR 823
Cdd:PRK11281 180 KGGKVGGKALRPSQrVLLQAEQALLNAQND----LQRKSLEGNTQL-----QDLLQ-KQRD-----YLTARIQRLEHQLQ 244
|
250 260 270
....*....|....*....|....*....|...
gi 1896085763 824 ALQEELSQAKCSSEEAQLEHAELQEQLHRANTD 856
Cdd:PRK11281 245 LLQEAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
819-1070 |
3.26e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 819 EEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtaelgiqvcALTVEKERVEEALACAVQELQDAKEAASREREG 898
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTL---------------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 899 LERQVAGLQQEKESLQEKLkaakaaagSLPGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAeimdYQSRLKNAGEECK 978
Cdd:PRK11281 103 LEALKDDNDEETRETLSTL--------SLRQLESRLAQTLDQLQNAQND----LAEYNSQLVS----LQTQPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 979 SLRGQLEEQGRQLQAAEEAVEKLKATQADMGEklscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYY 1058
Cdd:PRK11281 167 ANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ----AEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242
|
250
....*....|..
gi 1896085763 1059 NKLCQEVTNRER 1070
Cdd:PRK11281 243 LQLLQEAINSKR 254
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
747-917 |
3.31e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 747 LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcseregalqeeradeaqqrEEELRALQ 826
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-------------------TEKLLEYI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 827 EELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERqvaGL 906
Cdd:pfam15905 229 TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ---TL 305
|
170
....*....|.
gi 1896085763 907 QQEKESLQEKL 917
Cdd:pfam15905 306 NAELEELKEKL 316
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
538-1106 |
3.39e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.20 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 538 GKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEG--KLQALQADYQALQQRESAIQGSLASL 615
Cdd:pfam10174 173 PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDpaKTKALQTVIEMKDTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 616 EAEQASIRHLGD-----------QMEAsllaVRKAKEAMKAQMAEKEAILQSKEGE-----------------CQQ---- 663
Cdd:pfam10174 253 EDEVQMLKTNGLlhtedreeeikQMEV----YKSHSKFMKNKIDQLKQELSKKESEllalqtkletltnqnsdCKQhiev 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 664 LREEVEQCQQLAEARHRELRAL-------ESQCQQQTQLIEVLTAEKGQQGvgpptdNEARELAAQLALSQAQLEVHQGE 736
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALrlrleekESFLNKKTKQLQDLTEEKSTLA------GEIRDLKDMLDVKERKINVLQKK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 737 VQRLQAQVVD-------LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELlqcseregalqE 809
Cdd:pfam10174 403 IENLQEQLRDkdkqlagLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEEL-----------E 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 810 ERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVcaltveKERVEEALACAVQeLQDAK 889
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV------EQKKEECSKLENQ-LKKAH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 890 EAASREREGLE--RQVAGLQQEKESLQEKlkaAKAAAGSLPGLQAQLAQAEQRA----------QSLQEAAHQELNTLKF 957
Cdd:pfam10174 545 NAEEAVRTNPEinDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKndkdkkiaelESLTLRQMKEQNKKVA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 958 QLSAeiMDYQSRLKNAGEECKSLRGQLEE----QGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEcqaamlrKDKEG 1033
Cdd:pfam10174 622 NIKH--GQQEMKKKGAQLLEEARRREDNLadnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE-------KDGHL 692
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 1034 AALRedLERtQKELEKATTKIQEyynKLCQEVTNRERNdqkmLADLDDLNRTKKYLEERLIELLRDKDALWQK 1106
Cdd:pfam10174 693 TNLR--AER-RKQLEEILEMKQE---ALLAAISEKDAN----IALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1131-1179 |
3.48e-04 |
|
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).
Pssm-ID: 277283 [Multi-domain] Cd Length: 52 Bit Score: 39.71 E-value: 3.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1896085763 1131 CLDCKREFSWMVR-RHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACF 1179
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELpLPSSIYEPARVCDVCY 52
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-403 |
3.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 202 RERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEV--TQATQNTVKELQTCLQGLELGAA 279
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE---RREALQRLAEYSWDEidVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 280 EkeedyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDtkgRQEPIPSDAAQEMQELGEKL 359
Cdd:COG4913 686 D--------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEER 754
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1896085763 360 QALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 403
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARL---NRAEEELERAMRA 795
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
384-1101 |
4.36e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 384 VKELQLKEDARASLERLVKEMApLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSL 463
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEA-LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 464 TRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGP----ELPVAGEKNEALVPVNSSLQEAWGK 539
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeeELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 540 PEEEQRGLQE--AQLDDTKVQEGSQEEELRQANRELEK---ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLAS 614
Cdd:pfam02463 312 DEEKLKESEKekKKAEKELKKEKEEIEELEKELKELEIkreAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 615 LEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhRELRALESQCQQQTQ 694
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEEL---EKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 695 LIEVLTAEKgqQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------------AKMRAALDDQ 758
Cdd:pfam02463 469 KSEDLLKET--QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggriisahgrlgdlgvAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 759 DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEE 838
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 839 AQLEHAELQEQLHRANTDTAELGIQVcalTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLK 918
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGV---SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 919 AAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNageecKSLRGQLEEQGRQLQAAEEAV 998
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL-----KKEEKEEEKSELSLKEKELAE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 999 EKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLAD 1078
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740
....*....|....*....|...
gi 1896085763 1079 LDDLNRTKKYLEERLIELLRDKD 1101
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEE 881
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
894-1077 |
4.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 894 REREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA-AHQELNTLKFQLSAEIMDYQSRLKN 972
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 973 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKlscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1052
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|....*
gi 1896085763 1053 KIQEYYNKLCQEVTNRERNDQKMLA 1077
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLL 252
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
717-957 |
5.06e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 717 RELAAQLalsqaqLEVH-QGEVQRLqaqvvdLQAKM-RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQnealnrahv 794
Cdd:COG0497 119 RELGELL------VDIHgQHEHQSL------LDPDAqRELLDAFAGLEELLEEYREAYRAWRALKKELEEL--------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 795 qellqcseregalqEERADEAQQREEELRALQEELSQAKCSS-EEAQLE-------HAE-LQEQLHRA------NTDTAE 859
Cdd:COG0497 178 --------------RADEAERARELDLLRFQLEELEAAALQPgEEEELEeerrrlsNAEkLREALQEAlealsgGEGGAL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 860 LGIQVCALTVEK------------ERVEEALAcavqELQDAKEAASREREGLE------------------------RQV 903
Cdd:COG0497 244 DLLGQALRALERlaeydpslaelaERLESALI----ELEEAASELRRYLDSLEfdperleeveerlallrrlarkygVTV 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896085763 904 AGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR---------------AQSLQEAAHQELNTLKF 957
Cdd:COG0497 320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAElleaaeklsaarkkaAKKLEKAVTAELADLGM 388
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
545-766 |
5.08e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 545 RGLQEaQLDDTKVQEGSQEEELRQANReLEKELQNVVGRNqllegkLQALQADYQALQQRESAIQGSLASLEAEQASIRH 624
Cdd:PHA02562 177 RELNQ-QIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGEN------IARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 625 LGDQMEASLLAVRKAKEAMKAQMA--EKEAILQSKEGEC----QQLREEVEQC----QQLAEARHRELRALESQCQQQTQ 694
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCptctQQISEGPDRItkikDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896085763 695 LIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 766
Cdd:PHA02562 329 MDEFNEQSKKLLEL----KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1125-1179 |
6.08e-04 |
|
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.
Pssm-ID: 277279 [Multi-domain] Cd Length: 54 Bit Score: 39.21 E-value: 6.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 1125 DTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNnyvLSKHGGKKERCCRACF 1179
Cdd:cd15740 2 EKEKQTCKGCNESFNSITkRRHHCKQCGAVICGKCSE---FKDLASRHNRVCRDCF 54
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
885-1083 |
6.75e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 885 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG--SLPG------------------LQAQLAQAEQRAQSL 944
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEeaklllqqlselesqlaeARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 945 QEAAHQELNTLKFQL-SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQ 1023
Cdd:COG3206 246 RAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI------LASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1024 AAMLRKDKEGAALREDLERTQKELEKATTKIQEyYNKLCQEVTNRERNDQKMLADLDDLN 1083
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEAR 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
741-903 |
7.40e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 741 QAQVVDLQAkmraaLDDQ-DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERA----DEA 815
Cdd:COG1579 6 LRALLDLQE-----LDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 816 QQRE----EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEA 891
Cdd:COG1579 81 QLGNvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|..
gi 1896085763 892 ASREREGLERQV 903
Cdd:COG1579 161 LEAEREELAAKI 172
|
|
| GOLD_2 |
pfam13897 |
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ... |
1371-1416 |
8.27e-04 |
|
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is always found combined with lipid- or membrane-association domains.
Pssm-ID: 464028 Cd Length: 133 Bit Score: 40.93 E-value: 8.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1896085763 1371 LIPTTRCNSHKENIQGQLKVRTPGIYMLIFDNTFSRFVSKKVFYHL 1416
Cdd:pfam13897 85 IVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
201-910 |
9.18e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 201 LRERMQQLDRENQELRaavsQQGEQLQTERErgrTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGAAE 280
Cdd:pfam07111 61 LSQQAELISRQLQELR----RLEEEVRLLRE---TSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 281 KEEDYHTALRRLESMLQplaqeleatrdsldkknQHLASfpgwLAMAQQKA--DTASDTKGRQEPIPSdaaQEMQELGEK 358
Cdd:pfam07111 134 LEEGSQRELEEIQRLHQ-----------------EQLSS----LTQAHEEAlsSLTSKAEGLEKSLNS---LETKRAGEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 359 LQALERERtKVEEVNRQQSAQLEQLVKELQLKEdaraSLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtssweee 438
Cdd:pfam07111 190 KQLAEAQK-EAELLRKQLSKTQEELEAQVTLVE----SLRKYVGEQVPPEVHSQTWELERQELLDTMQHL---------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 439 laelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQ-----------------------KKQLIQDK 495
Cdd:pfam07111 255 ----QEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkkcrsllnrwrekvfalmvqlKAQDLEHR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 496 DHLSQQVGMLERLAgppgpELPVAGEKNEALvpVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANreLEK 575
Cdd:pfam07111 331 DSVKQLRGQVAELQ-----EQVTSQSQEQAI--LQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTAS--AEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 576 ELQNVVGrnqllegklqalqadyqALQQRESAIQGSLASLEAEQASIRHLGDQMEaslLAVRKAkEAMKAQMAEKEAILQ 655
Cdd:pfam07111 402 QLKFVVN-----------------AMSSTQIWLETTMTRVEQAVARIPSLSNRLS---YAVRKV-HTIKGLMARKVALAQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 656 SKEGEC------QQLREEVE-QCQQLAEARHRelraLESQCQQQTQLIevltaekgQQGVGpptdnEARElaaqlalsqa 728
Cdd:pfam07111 461 LRQESCpppppaPPVDADLSlELEQLREERNR----LDAELQLSAHLI--------QQEVG-----RARE---------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 729 qlevhQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAhvQELLQCSEREGALQ 808
Cdd:pfam07111 514 -----QGEAERQQLSEVAQQL-------EQELQRAQESLASVGQQLEVARQGQQESTEEAASLR--QELTQQQEIYGQAL 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 809 EERADEAQQReeelraLQEELSQAKCSSEEAQLEHAE----LQEQLHRAntdtaelgiqvcalTVEKERVEEalacaVQE 884
Cdd:pfam07111 580 QEKVAEVETR------LREQLSDTKRRLNEARREQAKavvsLRQIQHRA--------------TQEKERNQE-----LRR 634
|
730 740
....*....|....*....|....*.
gi 1896085763 885 LQDakEAASREREGLERQVAGLQQEK 910
Cdd:pfam07111 635 LQD--EARKEEGQRLARRVQELERDK 658
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
931-1064 |
9.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 931 QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGE-ECKSLRGQLEEQGRQLQAAEEAVEKLKatqadmg 1009
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENLDRKL------- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 1010 EKLSctsnhlaecqaamlRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQE 1064
Cdd:PRK12704 103 ELLE--------------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
781-1121 |
1.07e-03 |
|
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: 43.57 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 781 QLKEQNEALNrahvqELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQlhrantdtAEL 860
Cdd:pfam17380 263 QTMTENEFLN-----QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ--------AEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 861 GIQVcALTVEKERVeealacavqelqdakeAASREREgLER-QVAGLQQEKESL-QEKLKAAKAAAGSLPGLQAQLAQAE 938
Cdd:pfam17380 330 DRQA-AIYAEQERM----------------AMERERE-LERiRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 939 QRAQSLQEAAHqelntlKFQLSAEimDYQSRLKNAGEECKSLRGQLEE-QGRQLQAAEEA----VEKLKATQADMGEKLS 1013
Cdd:pfam17380 392 ERVRQELEAAR------KVKILEE--ERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEErareMERVRLEEQERQQQVE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1014 CTSNHLAECQAAMLRKDKEgaalredlERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE-- 1091
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKE--------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEErr 535
|
330 340 350
....*....|....*....|....*....|
gi 1896085763 1092 RLIELLRDKDALWQKSDALEFQQKLSAEER 1121
Cdd:pfam17380 536 REAEEERRKQQEMEERRRIQEQMRKATEER 565
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
718-888 |
1.07e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 718 ELAAQLALSQAQLEVhQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK--------EQNEAL 789
Cdd:cd22656 98 ELIDDLADATDDEEL-EEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEkalkdlltDEGGAI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 790 NRAHVQELLQcseregALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAE-LQEQLHRANTDTAELgiqvcalt 868
Cdd:cd22656 177 ARKEIKDLQK------ELEKLNEEYAAKLKAKIDELKALI-----ADDEAKLAAALrLIADLTAADTDLDNL-------- 237
|
170 180
....*....|....*....|
gi 1896085763 869 veKERVEEALAcAVQELQDA 888
Cdd:cd22656 238 --LALIGPAIP-ALEKLQGA 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
462-622 |
1.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 462 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMlerlagppgpelpvaGEKNEALVPVNSSLQEAwgkpe 541
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---------------GPDALPELLQSPVIQQL----- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 542 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVvgrNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 621
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
.
gi 1896085763 622 I 622
Cdd:COG3206 346 L 346
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
722-948 |
1.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 722 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvQELLqcs 801
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEER--REEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 802 eregalqEERADEAQQREEELRALQEELSQakcSSEEAQLEHAELQEQLHRANTDTAElgiQVCALTVEKERVEEALACA 881
Cdd:COG3883 89 -------GERARALYRSGGSVSYLDVLLGS---ESFSDFLDRLSALSKIADADADLLE---ELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 882 VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAA 948
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
540-697 |
1.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 540 PEEEQRGLQEAQLDDTKVQEgsqeeeLRQANRELEKELQNvvgrnqlLEGKLQALQADYQALQQRESAIQGSLASLEAEQ 619
Cdd:COG1579 2 MPEDLRALLDLQELDSELDR------LEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 620 ASIRHLGDQMEASLLAVRKAKE---------AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQ 690
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRNNKEyealqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
....*..
gi 1896085763 691 QQTQLIE 697
Cdd:COG1579 149 EELAELE 155
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
652-1001 |
1.61e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 652 AILQSKEGECQQLREEVE------QCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQ---GVGPPTDNEARELAAQ 722
Cdd:PRK10246 160 AFLNAKPKERAELLEELTgteiygQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSltaSLQVLTDEEKQLLTAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 723 LALSQA-QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAE--AVLR-------EHKTLVQQLKEQNEALN-R 791
Cdd:PRK10246 240 QQQQQSlNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRphweriqEQSAALAHTRQQIEEVNtR 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 792 AHVQELLQCSEREGALQEERADEAQQRE--------EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL-GI 862
Cdd:PRK10246 320 LQSTMALRARIRHHAAKQSAELQAQQQSlntwlaehDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLnAL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 863 QVCALTVEKERVEEALAcavqelQDAKEAASRER-EGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ----- 936
Cdd:PRK10246 400 PAITLTLTADEVAAALA------QHAEQRPLRQRlVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQrykek 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 937 ----AEQRAQSLQEAAHQELNTLKFQLSA---------------------EIMDYQSRL-------KNAGEECKSLRGQL 984
Cdd:PRK10246 474 tqqlADVKTICEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLdalekevKKLGEEGAALRGQL 553
|
410
....*....|....*..
gi 1896085763 985 EEQGRQLQAAEEAVEKL 1001
Cdd:PRK10246 554 DALTKQLQRDESEAQSL 570
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
601-1128 |
1.71e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 601 LQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKE--AMKAQMAEK-------EAILQSKEGECQQLREEV--- 668
Cdd:pfam10174 139 LEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAemqlghlEVLLDQKEKENIHLREELhrr 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 669 ----------EQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqGVGPPTDNEARELAAQLALSQA-----QLEVH 733
Cdd:pfam10174 219 nqlqpdpaktKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTN----GLLHTEDREEEIKQMEVYKSHSkfmknKIDQL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 734 QGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTlvqqLKEQNEALNRAHVQELLQCSEREGALQEERAD 813
Cdd:pfam10174 295 KQELSKKESELLALQTK----LETLTNQNSDCKQHIEVLKESLT----AKEQRAAILQTEVDALRLRLEEKESFLNKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 814 EAQQREEELRALQEELS----------------QAKCSSEEAQLEH-----AELQE-----QLHRANTDTAeLGIQVCAL 867
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlQKKIENLQEQLRDkdkqlAGLKErvkslQTDSSNTDTA-LTTLEEAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 868 TvEKERVEEALacavqelqdaKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEA 947
Cdd:pfam10174 446 S-EKERIIERL----------KEQREREDRERLEELESLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEH 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 948 AhQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQL---EEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQA 1024
Cdd:pfam10174 505 A-SSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1025 AM--LR--------KDKEGAALREDLERTQKELEKATTKIqeyynKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLI 1094
Cdd:pfam10174 584 LLgiLRevenekndKDKKIAELESLTLRQMKEQNKKVANI-----KHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLE 658
|
570 580 590
....*....|....*....|....*....|....
gi 1896085763 1095 ELLRDKDALWQKSDALefQQKLSAEERWLGDTEA 1128
Cdd:pfam10174 659 ELMGALEKTRQELDAT--KARLSSTQQSLAEKDG 690
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
871-1012 |
1.98e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 871 KERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE---KESLQEKLKaakaaaGSLPGLQAQLAQAEQRAQSLQea 947
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASlsaAEAERSRLQ------ALLAELAGAGAAAEGRAGELA-- 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896085763 948 ahQELNTLKfQLSAEIMdyqSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1012
Cdd:PRK09039 123 --QELDSEK-QVSARAL---AQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-419 |
1.99e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 185 DEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQAT-QNT 263
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 264 VKELQTCLQGLELGAAEKEEDYHTALRRLEsMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKgrqep 343
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAEL---------AALRAELEAERA----- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 344 ipsDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEAD 419
Cdd:COG4942 175 ---ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
653-860 |
2.05e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 653 ILQSKEGECQQLRE---------------EVEQCQQLAEARHRELRALESQCQQ-QTQLIEVltaEKGQQgvgpptdNEA 716
Cdd:pfam09787 19 ILQSKEKLIASLKEgsgvegldsstaltlELEELRQERDLLREEIQKLRGQIQQlRTELQEL---EAQQQ-------EEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 717 RELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAVLREHKTLVQQLKEQ--NEALNRAHV 794
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQltSKSQSSSSQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 795 QELlqcseregalqeeradeaqqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL 860
Cdd:pfam09787 166 SEL---------------------ENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKEL 210
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
540-962 |
2.30e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.20 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 540 PEEEQRGLQEAQLDDTKVQEGSQEEELRQAN-----RELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLAS 614
Cdd:COG5278 103 PEQQARLDELEALIDQWLAELEQVIALRRAGgleaaLALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 615 LEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQ 694
Cdd:COG5278 183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 695 LIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLRE 774
Cdd:COG5278 263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 775 HKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAN 854
Cdd:COG5278 343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 855 TDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQL 934
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*...
gi 1896085763 935 AQAEQRAQSLQEAAHQELNTLKFQLSAE 962
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAEL 530
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1130-1178 |
2.43e-03 |
|
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.
Pssm-ID: 277289 [Multi-domain] Cd Length: 47 Bit Score: 37.34 E-value: 2.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1896085763 1130 HCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvLSKHGGKKeRCCRAC 1178
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNC-----LSKEERGR-RRCRRC 44
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
690-990 |
2.72e-03 |
|
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: 42.42 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 690 QQQTQLIEVLTAEKGQQgvgpPTDNEARELAAQLALSQAQlEVHQGEVQRlQAQVVDLQAKM---------RAALDDQDK 760
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQ----EKEEKAREVERRRKLEEAE-KARQAEMDR-QAAIYAEQERMamerereleRIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 761 V-----QSQLSMAEAVLREHKTLVQQLKEQNE----ALNRAHVQELLQcSEREGALQEE-------RADEAQQREEELRA 824
Cdd:pfam17380 361 ElerirQEEIAMEISRMRELERLQMERQQKNErvrqELEAARKVKILE-EERQRKIQQQkvemeqiRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 825 LQEELSQakcSSEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLErqva 904
Cdd:pfam17380 440 LEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRK--KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE---- 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 905 glQQEKESLQEKlkaakaaagSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM---DYQSRLKNAGEECKSLR 981
Cdd:pfam17380 511 --EERKRKLLEK---------EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkatEERSRLEAMEREREMMR 579
|
....*....
gi 1896085763 982 GQLEEQGRQ 990
Cdd:pfam17380 580 QIVESEKAR 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
911-1121 |
2.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 911 ESLQEKLKAAKAAAGSLPGL---QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRgqleeq 987
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 988 grQLQAAEEAVEKLKATQADMgeklsctsNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtn 1067
Cdd:COG4717 123 --KLLQLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1896085763 1068 rERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1121
Cdd:COG4717 191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
751-1070 |
2.98e-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: 42.08 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 751 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREgALQEERADEAQQREEELRALQEELS 830
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE-EMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 831 QAKCSSEEAQLEHAELQEQL-----HRANTDTAELGIQVCALTVE---KERVEEALAcavqeLQDAKEAASREREGLERQ 902
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIqdleeQLDEEEAARQKLQLEKVTTEakiKKLEEDILL-----LEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 903 VAGLQQEKESLQEKLKAAKAAAGSLpglQAQLAQAEQRAQSlQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRG 982
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKH---EAMISDLEERLKK-EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 983 QLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQ-------AAMLRKDKEGAALREDLERTQKELEK---ATT 1052
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEALKTELEDtldTTA 316
|
330
....*....|....*...
gi 1896085763 1053 KIQEYYNKLCQEVTNRER 1070
Cdd:pfam01576 317 AQQELRSKREQEVTELKK 334
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
468-791 |
3.63e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 468 QFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEK--------------------NE 524
Cdd:PRK11281 63 QDLEQtlaLLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrqlesrlaqtldqlqnaQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 525 ALVPVNSSLQEAWGKPEEEQRGLQEAQ---------LDDTKVQEGSQEEELRQanrELEKELQNVVGRN----QLLEG-- 589
Cdd:PRK11281 143 DLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnlLKGGKVGGKALRPSQRV---LLQAEQALLNAQNdlqrKSLEGnt 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 590 KLQAL---QADYQALQQresaiqgslASLEAEQASIRHLGDQ--MEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 664
Cdd:PRK11281 220 QLQDLlqkQRDYLTARI---------QRLEHQLQLLQEAINSkrLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 665 REE-VEQCQQLAEARHRELRA---LESQCQQQTQLIEVLTAEKG---------QQGVGPPTDNEARELAAQLA-LSQAQL 730
Cdd:PRK11281 291 SQRlLKATEKLNTLTQQNLRVknwLDRLTQSERNIKEQISVLKGslllsrilyQQQQALPSADLIEGLADRIAdLRLEQF 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 731 EVHQ--GEVQRLQAQVVDLQAKMRAALDDQdkvqsqlsmaeavlrEHKTLVQQLKEQNEALNR 791
Cdd:PRK11281 371 EINQqrDALFQPDAYIDKLEAGHKSEVTDE---------------VRDALLQLLDERRELLDQ 418
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
930-1116 |
3.72e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 930 LQAQLAQAEQRAQ--SLQEAAHQELNTLKFQLsAEIMDYQSRLKnageeckSLRGQLEEQGRQLQAAEEAVEKLKATQ-- 1005
Cdd:PRK11281 41 VQAQLDALNKQKLleAEDKLVQQDLEQTLALL-DKIDRQKEETE-------QLKQQLAQAPAKLRQAQAELEALKDDNde 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1006 -----------ADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRE--RND 1072
Cdd:PRK11281 113 etretlstlslRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKalRPS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1896085763 1073 QKM-----LADLD---DLNRTKKYLEERLIELLRDK-DALWQKSDALEFQQKL 1116
Cdd:PRK11281 193 QRVllqaeQALLNaqnDLQRKSLEGNTQLQDLLQKQrDYLTARIQRLEHQLQL 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
462-697 |
4.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 462 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKD--HLSQQVGMLErlagppgpelpvageknEALVPVNSSLQEAwgk 539
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLL-----------------QQLSELESQLAEA--- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 540 peEEQRGLQEAQLDDTKVQEGSQEEELRQANREleKELQNVVGRNQLLEGKLQALQADYQ----ALQQRESAIQGSLASL 615
Cdd:COG3206 232 --RAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 616 EAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQ 692
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYEsllQRLEEARLAEALTVGN 387
|
....*
gi 1896085763 693 TQLIE 697
Cdd:COG3206 388 VRVID 392
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
749-886 |
4.13e-03 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 39.86 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 749 AKMRAALDDQDKVQSQLS--------MAEAVLREHKTLVQQL-KEQNEAlnRAHVQEL---LQCSEREGALQEERADEAQ 816
Cdd:pfam05335 23 AQAAAAEAAARQVKNQLAdkalqaakAAEAALAGKQQIVEQLeQELREA--EAVVQEEsasLQQSQANANAAQRAAQQAQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 817 QREEELRAL----QEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEAL---ACAVQELQ 886
Cdd:pfam05335 101 QQLEALTAAlkaaQANLENAEQVAAGAQQELAEKTQLLEAAKKRVERLQRQLAEARADLEKTKKAAykaACAAVEAK 177
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
882-1056 |
4.42e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 882 VQELQDAKEAASREREGLERQVAGLQQEKEslqeklkaakaaagslpGLQAQLAQAEQRAQSLqEAAHQELNTLKFQLSA 961
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELA-----------------ALEARLEAAKTELEDL-EKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 962 EIMDYQSRLKNAG--EECKSLRGQLEEQGRQLQAAE-------EAVEKLKATQADMGEKLSCTSNHLAECQAamlRKDKE 1032
Cdd:COG1579 74 RIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKA---ELDEE 150
|
170 180
....*....|....*....|....
gi 1896085763 1033 GAALREDLERTQKELEKATTKIQE 1056
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPP 174
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1121-1184 |
4.44e-03 |
|
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.
Pssm-ID: 277295 [Multi-domain] Cd Length: 76 Bit Score: 37.36 E-value: 4.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896085763 1121 RWLgdtEANHCLDCKREFSWMV-----------RRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLSE 1184
Cdd:cd15756 2 QWL---ESDSCQKCEQPFFWNIkqmwdtktlglRQHHCRKCGQAVCGKCSSKRSSYPIMGfeFQVRVCDSCFETIKD 75
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
179-704 |
4.53e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 179 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQEL---RAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWE 255
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 256 VTQATQNTVKELQ-TCLQGLELGaaEKEEDYHTALRRLESMLQPLAQELEATRDSLDKknqhlasfpgwlamAQQKADTA 334
Cdd:PRK03918 277 ELEEKVKELKELKeKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIKE--------------LEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 335 SDTKGRQEPIpsdaAQEMQELGEKLQALERERTKVEEVNRQQSA----QLEQLVKELQLKEDARASLERLVKEmapLQEE 410
Cdd:PRK03918 341 EELKKKLKEL----EKRLEELEERHELYEEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISK---ITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 411 LSGKGQEADQLWRRLQELlahtssweeELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQ 490
Cdd:PRK03918 414 IGELKKEIKELKKAIEEL---------KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 491 ----------LIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEalvpvnsSLQEAWGKPEEEQRGLQEaqlDDTKVQE- 559
Cdd:PRK03918 485 lekvlkkeseLIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-------KLKEKLIKLKGEIKSLKK---ELEKLEEl 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 560 GSQEEELRQANRELEKELQNVVGR--------NQLLEGKLQALQADYQ---ALQQRESAIQGSLASLEAEQASIrhlgDQ 628
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEEL----DK 630
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 629 MEASLLAVRKAKEAMKAQMAEKEAILQSKEGEcqQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKG 704
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
748-1013 |
4.88e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 748 QAKMRAALDDQDKVQSQLsmaeAVLREHKTLVQQLKEQNEALNRAhvQELLQCSERegalQEERADEAQQR----EEELR 823
Cdd:PRK11281 28 RAASNGDLPTEADVQAQL----DALNKQKLLEAEDKLVQQDLEQT--LALLDKIDR----QKEETEQLKQQlaqaPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 824 ALQEELSQAKCSSEE-----------AQLEH--AELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDake 890
Cdd:PRK11281 98 QAQAELEALKDDNDEetretlstlslRQLESrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 891 aasreregLERQVAGLQQEKE----SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDY 966
Cdd:PRK11281 175 --------IRNLLKGGKVGGKalrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 967 QS-----RLKnageeckslrgQLEEQGRQLQAAEEAVE----KLKATQADMGEKLS 1013
Cdd:PRK11281 247 QEainskRLT-----------LSEKTVQEAQSQDEAARiqanPLVAQELEINLQLS 291
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
779-1121 |
4.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 779 VQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEElsqaKCSSEEAQLEHAELQEQLHRANTDTA 858
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE----RNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 859 ELGIQVCAL--TVEKERVEEAL-ACAVQELQDAKEAA--SREREGLERQVAGLQQEKESLQEKLKAAKAAAgslpglQAQ 933
Cdd:PTZ00121 1275 EEARKADELkkAEEKKKADEAKkAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAA 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 934 LAQAEQRAQSLQEAAHQ----ELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKL-----KAT 1004
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKaeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAE 1428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 1005 QADMGEKLSCTSNHLAecQAAMLRKDKEGAALREDLERTQKELEKA-TTKIQEYYNKLCQEVTNRERNDQKMLADLDDLN 1083
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
330 340 350
....*....|....*....|....*....|....*....
gi 1896085763 1084 RTKKYLEE-RLIELLRDKDALWQKSDALEFQQKLSAEER 1121
Cdd:PTZ00121 1507 EAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
179-885 |
5.49e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 179 EALEGFDEMRLELDQLEVREKQLRE---RMQQLDRENQELRAAVSQQGEQLQTERErgrtaaednvrltclVAELQKQWE 255
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSEleqRLRQQQRAERLLAEFCKRLGKNLDDEDE---------------LEQLQEELE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 256 VTqatqntvkelqtcLQGLELGAAEKEEDYhTALRRLESMLQPLAQELEATRdsldkknqhlasfPGWLAmAQQKADTAS 335
Cdd:PRK04863 565 AR-------------LESLSESVSEARERR-MALRQQLEQLQARIQRLAARA-------------PAWLA-AQDALARLR 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 336 DTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKE--------LQLKEDARASL-----ERLVK 402
Cdd:PRK04863 617 EQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPggsedprlNALAERFGGVLlseiyDDVSL 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 403 EMAPLQEELSGKGQEA------DQLWRRLQELlahtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQ 476
Cdd:PRK04863 697 EDAPYFSALYGPARHAivvpdlSDAAEQLAGL--------------------------------EDCPEDLYLIEGDPDS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 477 VSQHVSDLEEQKKQLIQDkdhLSQQVGMLERLagppgPELPVAGEKN-----EALVPVNSSLQEAWGKPEEEQRGLQEAq 551
Cdd:PRK04863 745 FDDSVFSVEELEKAVVVK---IADRQWRYSRF-----PEVPLFGRAArekriEQLRAEREELAERYATLSFDVQKLQRL- 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 552 lddtkVQEGSQ--------------EEELRQANR---ELEKELQNVVGRNQLLEGKLQALQADYQALQQRESaiQGSLAS 614
Cdd:PRK04863 816 -----HQAFSRfigshlavafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGLSALNRLLP--RLNLLA 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 615 LEAEQASIRHLGDQMEASLLAVR--KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALesqcqqq 692
Cdd:PRK04863 889 DETLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL------- 961
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 693 TQLIEVLTAEKGQQGVGPPTDNEarELAAQLalsQAQLEvhQGEVQRLQAQVVDLQAKmrAALDDQDKVQSQLSMAEAVL 772
Cdd:PRK04863 962 TEVVQRRAHFSYEDAAEMLAKNS--DLNEKL---RQRLE--QAEQERTRAREQLRQAQ--AQLAQYNQVLASLKSSYDAK 1032
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 773 REhktLVQQLKEQNEALNRAHVQELlqcseregalqEERAdeAQQREEelraLQEELS--QAKCSSEEAQL-----EHAE 845
Cdd:PRK04863 1033 RQ---MLQELKQELQDLGVPADSGA-----------EERA--RARRDE----LHARLSanRSRRNQLEKQLtfceaEMDN 1092
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1896085763 846 LQEQLHRANTDtaelgiqvcaLTVEKERVEEALA--CAVQEL 885
Cdd:PRK04863 1093 LTKKLRKLERD----------YHEMREQVVNAKAgwCAVLRL 1124
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
681-795 |
6.71e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 681 ELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGEVQRL----------QAQVVDLQAK 750
Cdd:COG1566 84 ALAQAEAQLAAAEAQLARLEAELGAE-------AEIAAAEAQLAAAQAQLDLAQRELERYqalykkgavsQQELDEARAA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1896085763 751 MRAALDDQDKVQSQLSMAEAVLREHKTLVQ---QLKEQNEALNRAHVQ 795
Cdd:COG1566 157 LDAAQAQLEAAQAQLAQAQAGLREEEELAAaqaQVAQAEAALAQAELN 204
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
542-1002 |
7.24e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 542 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 621
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 622 IRHLGD--QMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEV- 698
Cdd:pfam05557 172 IKELEFeiQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLe 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 699 LTAEKGQQ------------GVGPPTDNEARELAAQLalsQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 766
Cdd:pfam05557 252 LEKEKLEQelqswvklaqdtGLNLRSPEDLSRRIEQL---QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 767 MAEAVLREHKTLVQQLKEQNEALN--RAHVQELLQCSEREGALQEERADEAQQREEELRALQEelSQAKCSSEEAQLEHA 844
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQRRVLLLTkeRDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQK--MQAHNEEMEAQLSVA 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 845 ELQEQLHRANTDTAELGIQVCAltvEKERVEEALACA--VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 922
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALR---QQESLADPSYSKeeVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 923 AAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1002
Cdd:pfam05557 484 KTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
713-886 |
7.64e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 713 DNEARELAAQLA-LSQAqLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrehktlvqqlkeqneALNR 791
Cdd:PRK09039 52 DSALDRLNSQIAeLADL-LSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAG-----------------AGAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 792 AhvqellqcSEREGALQEERADEAQQREEELRalQEELSQAKCSSEEAQLehAELQEQLHRANTDTAELGIQVCALtveK 871
Cdd:PRK09039 114 A--------EGRAGELAQELDSEKQVSARALA--QVELLNQQIAALRRQL--AALEAALDASEKRDRESQAKIADL---G 178
|
170
....*....|....*
gi 1896085763 872 ERVEEALACAVQELQ 886
Cdd:PRK09039 179 RRLNVALAQRVQELN 193
|
|
| RUN |
pfam02759 |
RUN domain; This domain is present in several proteins that are linked to the functions of ... |
49-133 |
8.13e-03 |
|
RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.
Pssm-ID: 460679 Cd Length: 134 Bit Score: 38.02 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 49 LEYLLQ------FDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRT---SLGKGRAFIRYSLVHQRLAD 119
Cdd:pfam02759 6 LEALLShglkrsSLLILRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNEKLLDQ 85
|
90
....*....|....
gi 1896085763 120 TLQQCFMNTKVTRR 133
Cdd:pfam02759 86 WLKLLLSNKELLSE 99
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
535-677 |
8.32e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 535 EAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGslAS 614
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA--AA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896085763 615 LEAEQASIRHLGDQMEASLLAVRKAKEAMK---AQMAEKEAILQSKEGECQQLREEVEQCQQLAEA 677
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAEAKKkaeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
729-958 |
8.32e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 729 QLEVHQGEVQRLQAQVVD-LQAKMRAaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQ--NEALNRAHV----------Q 795
Cdd:PRK10929 31 ELEQAKAAKTPAQAEIVEaLQSALNW-LEERKGSLERAKQYQQVIDNFPKLSAELRQQlnNERDEPRSVppnmstdaleQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 796 ELLQCSERegaLQEErADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG-IQVCALTVE---- 870
Cdd:PRK10929 110 EILQVSSQ---LLEK-SRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAqAQLTALQAEsaal 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896085763 871 KERVEE-----ALACAVQELQDAK-EAASREREGLERQVAGL--------QQEKESLQEKLKAAKAAAGSLP-GLQAQLA 935
Cdd:PRK10929 186 KALVDElelaqLSANNRQELARLRsELAKKRSQQLDAYLQALrnqlnsqrQREAERALESTELLAEQSGDLPkSIVAQFK 265
|
250 260
....*....|....*....|...
gi 1896085763 936 QAEQRAQSLQEAAhQELNTLKFQ 958
Cdd:PRK10929 266 INRELSQALNQQA-QRMDLIASQ 287
|
|
|