|
Name |
Accession |
Description |
Interval |
E-value |
| RUN_FYCO1 |
cd17698 |
RUN domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
15-124 |
2.43e-71 |
|
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: 235.36 E-value: 2.43e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 15 FDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDW 94
Cdd:cd17698 49 FDQKEKTTLLGGRKDYWDYFCECLAKVKGLNDGIRFVKSLKEVRTSLGKGRAFIRYSLVHQRLADTLQQCVMNGKVTSDW 128
|
90 100 110
....*....|....*....|....*....|
gi 1894925300 95 YYARSPFLQPKLSSDIVGQLYELTEVQFDL 124
Cdd:cd17698 129 YYPRSVFLNHKYSSDIINSLYDLNEVQFDL 158
|
|
| RUN_RUFY4 |
cd17697 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; ... |
14-124 |
1.35e-47 |
|
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: 166.89 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 14 KFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSD 93
Cdd:cd17697 40 QFDQKEKKSFFGSRKDYWDFLCLCLNRHRGGTEGIHFVNSTDKLKTPLGKGRAFIRYCLVQQQLAESLQLCLLNPELTGE 119
|
90 100 110
....*....|....*....|....*....|.
gi 1894925300 94 WYYARSPFLQPKLSSDIVGQLYELTEVQFDL 124
Cdd:cd17697 120 WYYARSPFLSPELRSDILDSLYELNGVNFDL 150
|
|
| RUN_RUFY4_like |
cd17682 |
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ... |
15-124 |
5.03e-41 |
|
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: 148.14 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 15 FDQKEKATLLGNKKDYWDYFCACLAKV----KGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKV 90
Cdd:cd17682 37 KGLKEKVSLGGRRKDYWDWLEELLKKLnkipKSLSDAVKFVKSCKKVKTNQGRGRLFIRYALNKKCLHDPVQQLVKNPKL 116
|
90 100 110
....*....|....*....|....*....|....
gi 1894925300 91 TSDWYYARSPFLQPKLSSDIVGQLYELTEVQFDL 124
Cdd:cd17682 117 LSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
|
|
| FYVE_FYCO1 |
cd15726 |
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ... |
1130-1187 |
2.50e-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: 131.53 E-value: 2.50e-36
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1187
Cdd:cd15726 1 WQDDTDVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGGKKERCCKACF 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-1010 |
3.31e-29 |
|
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: 127.09 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 203 EVREKQLR---ERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCL 279
Cdd:TIGR02168 221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 280 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPSDAAQE 359
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 360 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQ-LKEDARASLERLVK-EMAPLQEELSGKGQEADQLWRRLQELL 437
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 438 AHTSSweeeLAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLER-- 515
Cdd:TIGR02168 461 EALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGye 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 516 ----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQE--EELRQANRELEK 583
Cdd:TIGR02168 537 aaieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 584 ELQNVVGRNQLLEGKLQALQadyqalQQRESAIQGSLASLEAEQASIRHL----GDQMEASLLA-------VRKAKEAMK 652
Cdd:TIGR02168 617 ALSYLLGGVLVVDDLDNALE------LAKKLRPGYRIVTLDGDLVRPGGVitggSAKTNSSILErrreieeLEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 653 AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLA 732
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL------SKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 733 LSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLkeqnealnrahvQELLQCSERE 812
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL------------RERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 813 GALQEERADEAQQREEELRALQEELSqakcsseeaqLEHAELQEQLhrantdtAELGIQVCALTVEKERVEEALAcavqE 892
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLA----------AEIEELEELI-------EELESELEALLNERASLEEALA----L 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 893 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM 972
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQ----------LELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
810 820 830
....*....|....*....|....*....|....*...
gi 1894925300 973 DYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1010
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: ... |
1129-1192 |
4.12e-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: 4.12e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1129 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL---SKHGGKKERCCRACFQKLSE 1192
Cdd:pfam01363 2 VWVPDSSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISllpELGSNKPVRVCDACYDTLQK 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-1104 |
4.18e-25 |
|
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: 113.61 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 362 ELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEdarasLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTS 441
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 442 SWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPG 521
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 522 PELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQ------EAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQ-L 594
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 595 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLRE 674
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 675 EVEQCQQLA----------EARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELA---------AQLALSQ 735
Cdd:TIGR02168 511 LLKNQSGLSgilgvlseliSVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsikgTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 736 AQLEVHQGEVQRLQAQVVDLQAKMRAALDD-------QDKVQSQLSMAEAvLREHKTLV---------------QQLKEQ 793
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKK-LRPGYRIVtldgdlvrpggvitgGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 794 NEALNRAhvQELLQCsEREGALQEERADEAQQR----EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 869
Cdd:TIGR02168 670 SSILERR--REIEEL-EEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 870 IQVCALTVEKERVE---EALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 946
Cdd:TIGR02168 747 ERIAQLSKELTELEaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 947 QRAQSLQEAAHQELNTLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCT 1023
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1024 SNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnrERNDQKMLADLDDLNRTKKYLEERLIE 1103
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA---EALENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 1894925300 1104 L 1104
Cdd:TIGR02168 984 L 984
|
|
| FYVE |
smart00064 |
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ... |
1129-1191 |
2.24e-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: 2.24e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 1129 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLS 1191
Cdd:smart00064 3 HWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGieRPVRVCDDCYENLN 67
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
549-1059 |
3.84e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 549 EEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA 628
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 629 SIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV-EQCQQLAEARHRELRALESQCQQQTQLIEVL 707
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 708 TAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAqvvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLV 787
Cdd:COG1196 407 EAEEALL------ERLERLEEELEELEEALAELEEEEEEEEEA----LEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 788 QQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ-AKCSSEEAQLEHAELQEQLHRANTDTA 866
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVlIGVEAAYEAALEAALAAALQNIVVEDD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 867 ELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAE 946
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 947 QRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEcKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1026
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL-LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
490 500 510
....*....|....*....|....*....|...
gi 1894925300 1027 LAECQAAMLRKDKEGAALREDLERTQKELEKAT 1059
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-923 |
3.18e-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: 101.29 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 186 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaedNVRLTCLVAELQKQWEVT 265
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 266 QATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 345
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 346 KGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE---------QLVKELQLKEDARASLERLVKEMAPLQ 416
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelqaELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 417 EELSGKGQEADQLWRRLQEL---LAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQF-------LETQLAQVS 486
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVdegyeaaIEAALGGRL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 487 QH--VSDLEEQKKQLIQDKDHLSQQVGML---------------ERLAGPPG------------PELPVAGEKNEALVPV 537
Cdd:TIGR02168 548 QAvvVENLNAAKKAIAFLKQNELGRVTFLpldsikgteiqgndrEILKNIEGflgvakdlvkfdPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 538 NSSLQEAWGKPEEEQRGLQEAQLDDTKV-----------------QEGSQE--------EELRQANRELEKELQNVVGRN 592
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssiLERRREieeleekiEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 593 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 672
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 673 REEVEQCQQLAEARHRELRALESQCQQQTqlIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQV 752
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESL----ERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 753 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRaHVQELlqcserEGALQEERADEAQQREEELRA 832
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-KRSEL------RRELEELREKLAQLELRLEGL 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 833 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEaasrEREGLERQVA 912
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKE----RYDFLTAQKE 1010
|
810
....*....|.
gi 1894925300 913 GLQQEKESLQE 923
Cdd:TIGR02168 1011 DLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
360-1062 |
1.60e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.39 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 360 MQELGEKLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARaslerlvkemapLQEELSGKGQEADQLWRRLQELLAH 439
Cdd:COG1196 195 LGELERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRE------------LEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 440 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmlerlagp 519
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 520 pgpelpvAGEKNEALVPVNSSLQEAwgkpeEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQnvvgRNQLLEGKL 599
Cdd:COG1196 332 -------LEELEEELEELEEELEEA-----EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE----ELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 600 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 679
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 680 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 759
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 760 RAALDDQDKVQSQlsmAEAVLREHKtlvqQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 839
Cdd:COG1196 549 QNIVVEDDEVAAA---AIEYLKAAK----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 840 AkcssEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcAVQELQDAKEAASREREGLERQVAGLQQEKE 919
Cdd:COG1196 622 L----LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG-SRRELLAALLEAEAELEELAERLAEEELELE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 920 SLQEKLKAAKAAagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEEckslrgqlEEQGRQL 999
Cdd:COG1196 697 EALLAEEEEERE------LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE--------LPEPPDL 762
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 1000 QAAEEAVEKLKATQADMGeklscTSNHLAECQAAMLRKDKEG-AALREDLERTQKELEKATTKI 1062
Cdd:COG1196 763 EELERELERLEREIEALG-----PVNLLAIEEYEELEERYDFlSEQREDLEEARETLEEAIEEI 821
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
207-821 |
1.36e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 207 KQLRERMQQLDREnqELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGA 286
Cdd:COG1196 216 RELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 287 AEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASfpgwlamAQQKADTASDtkgrqepipsDAAQEMQELGEK 366
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-------LEEELEELEE----------ELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 367 LQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEE 446
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 447 LAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAGPPGPELPV 526
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 527 AGEKNEALVPVNSSLQEAWGK------PEEEQRGLQEAQLDDTKVQEGSQEEELRQ---------ANRELEKELQNVVGR 591
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAayeaalEAALAAALQNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 592 NQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQ 671
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 672 LREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQ 751
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEER-----------------ELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 752 VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHktlVQQLKEQNEAL---NRAHVQELLQCSEREGALQEERAD 821
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERE---LERLEREIEALgpvNLLAIEEYEELEERYDFLSEQRED 806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
780-1126 |
2.41e-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: 91.66 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 780 LREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLH 859
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 860 RANTDTAELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQ 939
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERL----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEE----------LK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 940 AQLAQAEQRAQSLqEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1019
Cdd:TIGR02168 351 EELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1020 LS-----CTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTK 1094
Cdd:TIGR02168 430 LEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-AQLQARLDSLERLQENLEGFSEGV 508
|
330 340 350
....*....|....*....|....*....|..
gi 1894925300 1095 KYLEERLIELLRDKDALWQKsdaLEFQQKLSA 1126
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSEL---ISVDEGYEA 537
|
|
| FYVE_like_SF |
cd00065 |
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ... |
1138-1187 |
9.32e-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: 78.34 E-value: 9.32e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 1138 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1187
Cdd:cd00065 1 RCMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSfgSGKPVRVCDSCY 52
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
244-921 |
1.32e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 244 AAEDN-VRLTCLVAELQKQWEV--TQATQ-NTVKELQTCLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSL 318
Cdd:COG1196 183 ATEENlERLEDILGELERQLEPleRQAEKaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 319 DKKNQHLASfpgwLAMAQQKADTASDTKGrqepipsdaaQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL- 397
Cdd:COG1196 263 AELEAELEE----LRLELEELELELEEAQ----------AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 398 ---KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekelleqevrSLTRQ 474
Cdd:COG1196 329 eeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---------------------ELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 475 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvageknealvpvnsslqeawgkpEEEQRG 554
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERL------------------------------------------EEELEE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 555 LQEAQLddtkvQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 634
Cdd:COG1196 426 LEEALA-----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 635 DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALEsqcqqqtQLIEVLTAEKGQQ 714
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA-------AAIEYLKAAKAGR 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 715 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 794
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 795 EALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKcSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 874
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL-AEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1894925300 875 LTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESL 921
Cdd:COG1196 733 EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
649-1021 |
2.35e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 649 EAMKAQMAEKEAILQSKEGECQQLREEVEQcqqlAEaRHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdnEARELA 728
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEK----AE-RYRELKEELKELEAELLLLKLRELEA-----------ELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 729 AQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAHVQEllqc 808
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERL---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 809 sEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvEKERVEEALAC 888
Cdd:COG1196 319 -EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 889 AVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLS 968
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE----------LEEALAELEEEEEEEEEALEEAAEEEA-ELE 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 969 AEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLS 1021
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| FYVE_PIKfyve_Fab1 |
cd15725 |
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ... |
1130-1188 |
3.93e-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: 76.59 E-value: 3.93e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACFQ 1188
Cdd:cd15725 2 WMPDSSCKECYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGdlRVCTYCCK 62
|
|
| FYVE_EEA1 |
cd15730 |
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ... |
1129-1187 |
4.49e-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: 4.49e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925300 1129 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1187
Cdd:cd15730 2 KWADDEEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSKKPVRVCDACF 60
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
781-1100 |
6.74e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 781 REHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHR 860
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 861 ANTDTAELGIQvcaLTVEKERVEEALAcAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQA 940
Cdd:COG1196 293 LLAELARLEQD---IARLEERRRELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 941 QLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1020
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1021 SCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLcQEVTNRERNDQKMLADLDDLNRTKKYLEER 1100
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-AEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
362-1101 |
4.35e-16 |
|
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: 84.35 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 362 ELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQL-KEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAht 440
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQALLKEKREYEGYELLKeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 441 ssweEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLI-------QDKDHLSQQVGML 513
Cdd:TIGR02169 273 ----LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeidkllAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 514 ERLAGPPGPELPVAGEKNEALV----PVNSSLQEAWGKPEEEQRGLQEAQ------------LDDTKVQEGSQEEELRQA 577
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRaeleEVDKEFAETRDELKDYREKLEKLKreinelkreldrLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 578 -------NRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 650
Cdd:TIGR02169 429 iagieakINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 651 MKAQMAEKEAILQSKEGecqqlreeveQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGV--------GPPTDN 722
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHG----------TVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIellkrrkaGRATFL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 723 EARELAAQLALSQAqleVHQGEVQRLQAQVVDLQAKMRAA----LDDQDKVQSqLSMAEAVLREHK--TLVQQLKEQNEA 796
Cdd:TIGR02169 579 PLNKMRDERRDLSI---LSEDGVIGFAVDLVEFDPKYEPAfkyvFGDTLVVED-IEAARRLMGKYRmvTLEGELFEKSGA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 797 LNRAHVQ-------------ELLQCSEREGALQEERADEAQQREE---ELRALQEELSQAKCSSEEAQLEHAELQEQLHR 860
Cdd:TIGR02169 655 MTGGSRAprggilfsrsepaELQRLRERLEGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 861 ANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEK-ESLQEKLKAAKAAAGSLPGLQ 939
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 940 AQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1019
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQ----EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1020 LSCTSNHLAECQaamlRKDKEGAALREDLERTQKELeKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE 1099
Cdd:TIGR02169 891 RDELEAQLRELE----RKIEELEAQIEKKRKRLSEL-KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
..
gi 1894925300 1100 RL 1101
Cdd:TIGR02169 966 EI 967
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
556-1111 |
4.88e-16 |
|
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: 84.34 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 556 QEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 632
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 633 LGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHR------------------------ 688
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqletlrskvaqlelqia 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 689 ----ELRALESQCQQQTQLIEVLTAEKGQQGvGPPTDNEARELAAQLALS-------QAQLEVHQGEVQRLQAQVVDLQA 757
Cdd:TIGR02168 397 slnnEIERLEARLERLEDRRERLQQEIEELL-KKLEEAELKELQAELEELeeeleelQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 758 KMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAH-----VQELLQCSER-----EGALQE---------- 817
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvLSELISVDEGyeaaiEAALGGrlqavvvenl 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 818 ---ERADEAQQREEELRALQEELSQAKC----SSEEAQLEHAE--------------------------------LQEQL 858
Cdd:TIGR02168 556 naaKKAIAFLKQNELGRVTFLPLDSIKGteiqGNDREILKNIEgflgvakdlvkfdpklrkalsyllggvlvvddLDNAL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 859 HRANTDTAELGI-------------------QVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 919
Cdd:TIGR02168 636 ELAKKLRPGYRIvtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 920 SLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGE---ECKSLRGQLEEQ- 995
Cdd:TIGR02168 716 QLRKELEELSRQ---ISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELEERLEEAEEelaEAEAEIEELEAQi 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 996 ----------GRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT---KI 1062
Cdd:TIGR02168 792 eqlkeelkalREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieEL 871
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1894925300 1063 QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL 1111
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
353-1083 |
1.07e-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: 83.09 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 353 PSDAAQEMQELgEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKED--------ARASLERLVKEMAPLQEELSGKGQ 424
Cdd:TIGR00618 162 SKEKKELLMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctpcmpdtYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 425 EADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLetQLAQVSQHVSDLEEQKKQLIQDkd 504
Cdd:TIGR00618 241 SHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTE-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 505 hLSQQVGMLERLAGPPGPELpvageKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLD--DTKVQEGSQEEELRQANRELE 582
Cdd:TIGR00618 316 -LQSKMRSRAKLLMKRAAHV-----KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 583 KELQNVVGRNQLLEgKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASL---LAVRKAKEAMKAQMAEKE 659
Cdd:TIGR00618 390 TLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAItctAQCEKLEKIHLQESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 660 AILQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEvLTAEKGQQGVGPPTDNEARELAAQLALSQAQLE 739
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLELQ--EEPCPLCGSCIH-PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 740 VHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 819
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 820 ADeaQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAntdtaelgiqvcALTVEKERVEEALACAVQELQDAKEA 899
Cdd:TIGR00618 626 DL--QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL------------SIRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 900 ASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQ-RAQSLQEAAHQELNTLKFQLSAEIMDYQSRL 978
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDaLNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 979 --KNAGEECKSLRGQLEEQGRQLqaaEEAVEKLKATQADMGEKLsctsnhlaecQAAMLRKDKEGAALREDLERTQKELE 1056
Cdd:TIGR00618 772 aaLQTGAELSHLAAEIQFFNRLR---EEDTHLLKTLEAEIGQEI----------PSDEDILNLQCETLVQEEEQFLSRLE 838
|
730 740
....*....|....*....|....*..
gi 1894925300 1057 KATTKIQEYYNKLCQEVTNRERNDQKM 1083
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLT 865
|
|
| FYVE_LST2 |
cd15731 |
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ... |
1129-1187 |
1.57e-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: 1.57e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 1129 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACF 1187
Cdd:cd15731 4 LWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCsSNSVPLPRYGqMKPVRVCNHCF 64
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
527-984 |
1.10e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 527 AGEKNEALVPV---NSSLQEAWgkpeeEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQNVVGRNQLLEGKLQAL 602
Cdd:COG4913 247 AREQIELLEPIrelAERYAAAR-----ERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 603 QADYQALQQRESAIQGS-LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQ 681
Cdd:COG4913 322 REELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 682 LAEARHRELRALESQCQQQ-TQLIEVLTAEKGQQGVGPPTDNEAR-ELAAQLALSQAQL-------EVHQGEV------- 745
Cdd:COG4913 402 ALEEALAEAEAALRDLRRElRELEAEIASLERRKSNIPARLLALRdALAEALGLDEAELpfvgeliEVRPEEErwrgaie 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 746 -------------QRLQAQVVDL--QAKMRAALDDQdKVQSQLSMAEAVLREHKTLVQQLK-EQNEAlnRAHVQELLQ-- 807
Cdd:COG4913 482 rvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYE-RVRTGLPDPERPRLDPDSLAGKLDfKPHPF--RAWLEAELGrr 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 808 ----CSEREGALQEER----------------------------------ADEAQQREEELRALQEELSQAKCSSEEAQL 849
Cdd:COG4913 559 fdyvCVDSPEELRRHPraitragqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 850 EHAELQEQLHRANT---------DTAELGIQVCALTVEKERVE------EALACAVQELQDAKEAASREREGLERQVAGL 914
Cdd:COG4913 639 ELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRL 718
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 915 QQEKESLQEKLKAAKAAAGSLPGLQAQLAQA---EQRAQSLQEAAHQElntLKFQLSAEIMDYQSRLKNAGEE 984
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERE---LRENLEERIDALRARLNRAEEE 788
|
|
| FYVE_endofin |
cd15729 |
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ... |
1130-1190 |
1.38e-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: 69.69 E-value: 1.38e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1190
Cdd:cd15729 7 WVPDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCSlKARLEYLDNKEARVCVPCYQTL 68
|
|
| RUN |
cd17671 |
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ... |
24-124 |
1.58e-14 |
|
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: 72.46 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 24 LGNKKDYWDYFCACLAKVKGANDG--IRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPF 101
Cdd:cd17671 52 GGGKVSFWDFLEALEKLLPAPSLKqaIRDINSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALL 131
|
90 100
....*....|....*....|...
gi 1894925300 102 LQPKLSSDIVGQLYELTEVQFDL 124
Cdd:cd17671 132 RDPEEAELFLSLLVGLSSLDFNL 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-1105 |
4.04e-14 |
|
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: 77.80 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 188 ALEGFDEMRLELDQLEVREKQLRERMQQLdrenqelraavsqQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA 267
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERL-------------RREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 268 TQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKnqhLASFPGWLAMAQQKADtasdtkg 347
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIA------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 348 rqepipsDAAQEMQELGEKLQALERERTKVEEvnrqqsaQLEQLVKELqlkedaraslERLVKEMAPLQEELSGKGQEAD 427
Cdd:TIGR02169 312 -------EKERELEDAEERLAKLEAEIDKLLA-------EIEELEREI----------EEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 428 QLWRRLQELLAHTSSWEeelaelrREKKQQQEEKELLEQEVRSLTRQ-------LQFLETQLAQVSQHVSDLEEQKKQLI 500
Cdd:TIGR02169 368 DLRAELEEVDKEFAETR-------DELKDYREKLEKLKREINELKREldrlqeeLQRLSEELADLNAAIAGIEAKINELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 501 QDKDHLSQQVGMLERlagppgpELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE--AQLDDTKVQEGSQEEELRQAN 578
Cdd:TIGR02169 441 EEKEDKALEIKKQEW-------KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelAEAEAQARASEERVRGGRAVE 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 579 RELEKELQNVVGrnqlLEGKLQALQADYQAlqQRESAIQGSLASLEAE-----QASIRHLGDQM--EASLLAVRKakeaM 651
Cdd:TIGR02169 514 EVLKASIQGVHG----TVAQLGSVGERYAT--AIEVAAGNRLNNVVVEddavaKEAIELLKRRKagRATFLPLNK----M 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 652 KAQMAEKEAIlqSKEGECQQLREEVEQCQQLAEA------------RHRELRALESQCQQQTQLIEVL----------TA 709
Cdd:TIGR02169 584 RDERRDLSIL--SEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvveDIEAARRLMGKYRMVTLEGELFeksgamtggsRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 710 EKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQ 789
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE---QEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 790 LKEQnealnRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAELQeqlhrantdtaELG 869
Cdd:TIGR02169 739 LEEL-----EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----NDLEARLSHSRIP-----------EIQ 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 870 IQVCALTVEKERVEEALACAVQELQD---AKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAE 946
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN----------LNGKKEELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 947 QRAQSLQeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH 1026
Cdd:TIGR02169 868 EELEELE---------------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1027 LAECQAAmLRKDKEGAALREDLERTQKELEKATTKIQEYynklcQEVTNRERND-QKMLADLDDLNRTKKYLEERLIELL 1105
Cdd:TIGR02169 933 LSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIRAL-----EPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| FYVE_RUFY1_like |
cd15721 |
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ... |
1130-1187 |
5.06e-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: 67.79 E-value: 5.06e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1187
Cdd:cd15721 1 WADDKEVTHCQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSAKPVRVCDTCY 58
|
|
| FYVE_MTMR3 |
cd15732 |
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ... |
1129-1187 |
5.07e-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: 5.07e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 1129 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACF 1187
Cdd:cd15732 1 RWVPDHLAASCYGCEREFWLASRKHHCRNCGNVFCGSCCNQklPVPSQQLFEPSRVCKSCF 61
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
187-739 |
5.15e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 187 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQ 266
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 267 ATQNTVKELQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFpgwLAMAQQKADTASDTK 346
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 347 GRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEA 426
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 427 DQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTrqlqfLETQLAQVSQH-VSDLEEQKKQLIQDkdh 505
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-----LEAALAAALQNiVVEDDEVAAAAIEY--- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 506 lsqqvgmLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRElekel 585
Cdd:COG1196 566 -------LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE----- 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 586 qNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgdQMEASLLAVRKAKEAMKAQMAEKEAILQSK 665
Cdd:COG1196 634 -AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE--LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 666 EGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqgvgPPTDNEARELAAQLALSQAQLE 739
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE-------LPEPPDLEELERELERLEREIE 777
|
|
| FYVE_MTMR4 |
cd15733 |
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ... |
1130-1187 |
1.48e-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: 1.48e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 1130 WLGDTEANHCLDCKREFsWMV-RRHHCRICGRIFCYYCCNnyvlSKHGGKKE------RCCRACF 1187
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; ... |
1127-1172 |
1.54e-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: 1.54e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1894925300 1127 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVL 1172
Cdd:cd15727 1 EPPWVPDKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVP 46
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
471-1127 |
5.72e-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: 73.95 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 471 LTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpelpvagekneaLVPVNSSLQEawgKPEE 550
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL-----------------LEELNKKIKD---LGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 551 EQRGLQEaQLDDTKVQEGSQEEELRQANRELEKelqnvvgrnqlLEGKLQALQADYqalqqreSAIQGSLASLEAEQASI 630
Cdd:TIGR02169 288 EQLRVKE-KIGELEAEIASLERSIAEKERELED-----------AEERLAKLEAEI-------DKLLAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 631 RHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAE 710
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 711 -KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 789
Cdd:TIGR02169 429 iAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 790 LKEQNEALNR------AHVQELLQCSERE---------GALQ------EERADEAQQREEE----------LRALQEELS 838
Cdd:TIGR02169 509 GRAVEEVLKAsiqgvhGTVAQLGSVGERYataievaagNRLNnvvvedDAVAKEAIELLKRrkagratflpLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 839 QAKCSSEEAQLEHA----ELQEQLHRA------------NTDTA-ELGIQVCALTVEKERVE-----------EALACAV 890
Cdd:TIGR02169 589 DLSILSEDGVIGFAvdlvEFDPKYEPAfkyvfgdtlvveDIEAArRLMGKYRMVTLEGELFEksgamtggsraPRGGILF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 891 QELQDAKEAASRER-EGLERQVAGLQQEKESLQ----EKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHqelntlkf 965
Cdd:TIGR02169 669 SRSEPAELQRLRERlEGLKRELSSLQSELRRIEnrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE-------- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 966 QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADmgEKLSCTSNHLAECQAAMLRKDKEGAALR 1045
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1046 EDLERTQKELEKATTKIQEYYNK----------LCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDAL-WQK 1114
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQridlkeqiksIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeAQL 898
|
730
....*....|...
gi 1894925300 1115 SDALEFQQKLSAE 1127
Cdd:TIGR02169 899 RELERKIEELEAQ 911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
579-1143 |
7.71e-13 |
|
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: 73.61 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 579 RELEKELQNVVGRNQLLEGKLQALQADYQ-----ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKA 653
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 654 QMAEKEAI----LQSKEGECQQLREEVEQCQQLAEARHRELRalESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 729
Cdd:pfam15921 307 QARNQNSMymrqLSDLESTVSQLRSELREAKRMYEDKIEELE--KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 730 -------QLALSQAQ---------------------LEVHQGEVQRLQAQVVDLQAKMRAALDDQdkvQSQLSMAEAVLR 781
Cdd:pfam15921 385 dlhkrekELSLEKEQnkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQ---MAAIQGKNESLE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 782 EHKTLVQQLKEQNEALnRAHVQEL------LQCSERE-----GALQE-ERADEAQQRE------------EELRALQEE- 836
Cdd:pfam15921 462 KVSSLTAQLESTKEML-RKVVEELtakkmtLESSERTvsdltASLQEkERAIEATNAEitklrsrvdlklQELQHLKNEg 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 837 --LSQAKCSSEEAQLEHAE-------LQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQ------DAKEAAS 901
Cdd:pfam15921 541 dhLRNVQTECEALKLQMAEkdkvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkDKKDAKI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 902 REregLERQVAGLQQEKESLqeklkaakAAAGSlPGLQAQLAQAEQRAQSLQEA--AHQELNTLkfqlSAEIMDYQSRLK 979
Cdd:pfam15921 621 RE---LEARVSDLELEKVKL--------VNAGS-ERLRAVKDIKQERDQLLNEVktSRNELNSL----SEDYEVLKRNFR 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 980 NAGEECKSLRGQLEeqgRQLQAAEEAVEKLKATQADMgeklSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKAT 1059
Cdd:pfam15921 685 NKSEEMETTTNKLK---MQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1060 TK-------IQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL--IELLRDKDALwQKSDALEFQQKLSAEERW 1130
Cdd:pfam15921 758 TNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVanMEVALDKASL-QFAECQDIIQRQEQESVR 836
|
650
....*....|...
gi 1894925300 1131 LgdtEANHCLDCK 1143
Cdd:pfam15921 837 L---KLQHTLDVK 846
|
|
| FYVE_scVPS27p_like |
cd15760 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1135-1187 |
7.85e-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: 7.85e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 1135 EANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHGGKKERC--CRACF 1187
Cdd:cd15760 4 PDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIpLPHLGPLGVPQrvCDRCF 59
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-979 |
9.54e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 355 DAAQEMQELgekLQALERERTKVEEVnRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQeelsgkgqeadqLWRRLQ 434
Cdd:COG4913 225 EAADALVEH---FDDLERAHEALEDA-REQIELLEPIRELAERYAAARERLAELEYLRAALR------------LWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 435 ELLAhtssWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVS-QHVSDLEEQKKQLIQDKDHLSQQVGML 513
Cdd:COG4913 289 RLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 514 ERLAGPPGPELPVAGEKNEALVPVNSSLQEAWgkpeEEQRGLQEAQLDDTKVqegsQEEELRQANRELEKELQNVVGRNQ 593
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEAL----EEELEALEEALAEAEA----ALRDLRRELRELEAEIASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 594 LLEGKLQALQADY-QALQQRES--------------------AIQGSLASL------EAEQAS-----IRHLGDQMEASL 641
Cdd:COG4913 437 NIPARLLALRDALaEALGLDEAelpfvgelievrpeeerwrgAIERVLGGFaltllvPPEHYAaalrwVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 642 LAVRKAKEAMKAQMAEKEAI---LQSKEGECQQ-LREEVEQ-----CQQLAEARHRELRALESQCQ--QQTQLievltAE 710
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSLagkLDFKPHPFRAwLEAELGRrfdyvCVDSPEELRRHPRAITRAGQvkGNGTR-----HE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 711 KGQQGVGPPT-----DNEAR--ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmRAALDDQDKVQSQLSMAEAVLREh 783
Cdd:COG4913 592 KDDRRRIRSRyvlgfDNRAKlaALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAERE- 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 784 ktlVQQLKEQNEALNRAHvQELLQCSEREGALQEERaDEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANT 863
Cdd:COG4913 670 ---IAELEAELERLDASS-DDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 864 DTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE-KESLQEKLKAAKAAAGSLPGLQAQL 942
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALL 821
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1894925300 943 AQ--------AEQR-AQSLQEAAHQELNTLKFQLSAEIMDYQSRLK 979
Cdd:COG4913 822 DRleedglpeYEERfKELLNENSIEFVADLLSKLRRAIREIKERID 867
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
821-1128 |
1.07e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 821 DEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEealacaVQELQDAKEAA 900
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE------LEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 901 SREREGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSLQEAAHQELNTLKfqlsAEIMDYQSRLKN 980
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL--------------EELEEELAELEEELEELEEELEELE----EELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 981 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1060
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925300 1061 KIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1128
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
179-1056 |
1.58e-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: 72.46 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 179 DLNSPLNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQT---ERERGRTAAEDNVRltclv 255
Cdd:pfam15921 60 ELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTklqEMQMERDAMADIRR----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 256 AELQKQWEVTQATQNTVKELQT--CLQGLELGAAEKE-EDYHTALRRLESMLQPLAQELEATRDSLDKK--------NQH 324
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAakCLKEDMLEDSNTQiEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmsTMH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 325 LASFPGWLAMAQQKADTA-SDTKGRQEPIPsdaaqemqelgEKLQALERE-RTKVEEVNRQQSAQLEQLVKELQLK---- 398
Cdd:pfam15921 215 FRSLGSAISKILRELDTEiSYLKGRIFPVE-----------DQLEALKSEsQNKIELLLQQHQDRIEQLISEHEVEitgl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 399 ----EDARASLERLVKEMAPLQEElsGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSltrQ 474
Cdd:pfam15921 284 tekaSSARSQANSIQSQLEIIQEQ--ARNQNSMYM-RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS---E 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 475 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgmlerlagppgpELPVAGEKNEALvpvnsslqeaWgkpeeeqrg 554
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREK--------------ELSLEKEQNKRL----------W--------- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 555 lqeaqldDTKVQEGSQEEELRqanRELEKELQNVvgrnQLLEGKLQALQADYQA-LQQRESAIQGSLASLEaeqaSIRHL 633
Cdd:pfam15921 405 -------DRDTGNSITIDHLR---RELDDRNMEV----QRLEALLKAMKSECQGqMERQMAAIQGKNESLE----KVSSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 634 GDQMEASLLAVRKAKEAMKAqmaeKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkGQ 713
Cdd:pfam15921 467 TAQLESTKEMLRKVVEELTA----KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 714 QGVGPPTDNEARELaaQLALSQAQLEVHQGEVQRLqAQVVDLQAKMRAALD-DQDKVQSQLSMAEAVLREHKTL------ 786
Cdd:pfam15921 542 HLRNVQTECEALKL--QMAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQEFKILkdkkda 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 787 -VQQLKEQNEALNRAHVQELLQCSEREGALQeeraDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT 865
Cdd:pfam15921 619 kIRELEARVSDLELEKVKLVNAGSERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 866 AELGIQVCALTVEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQA 945
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF----------LEEAMTNA 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 946 EQRAQSLQEAahqelntlKFQLSAEimdyqsrLKNAGEECKSLRGQLEeqgrQLQAAEeavEKLKATQADMGEKLSCTSN 1025
Cdd:pfam15921 761 NKEKHFLKEE--------KNKLSQE-------LSTVATEKNKMAGELE----VLRSQE---RRLKEKVANMEVALDKASL 818
|
890 900 910
....*....|....*....|....*....|.
gi 1894925300 1026 HLAECQAAMLRKDKEGAALREDLERTQKELE 1056
Cdd:pfam15921 819 QFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| FYVE_RUFY1 |
cd15758 |
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
1130-1186 |
1.76e-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: 63.93 E-value: 1.76e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1186
Cdd:cd15758 6 WLKDDEATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSC 62
|
|
| FYVE_Hrs |
cd15720 |
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ... |
1134-1190 |
2.17e-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: 63.17 E-value: 2.17e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925300 1134 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACFQKL 1190
Cdd:cd15720 3 KDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSsTIPKFGIEKEvRVCDPCYEKL 61
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
571-955 |
2.33e-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: 72.02 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 571 EEELRQANRELEKELQNVvGRNQLLEG----KLQALQAD------YQALQQRESAIQGSLASLEaeqasirhlgdqmeas 640
Cdd:TIGR02169 169 DRKKEKALEELEEVEENI-ERLDLIIDekrqQLERLRRErekaerYQALLKEKREYEGYELLKE---------------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 641 LLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQlievltaekgqqgvgppt 720
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------------------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 721 dNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEqnEALNRA 800
Cdd:TIGR02169 294 -EKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-------EIDKLLAEIEELEREIEEERKRRDKLTE--EYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 801 HVQELLQCSeregaLQEERADEAQQREEeLRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQvcaLTVEKE 880
Cdd:TIGR02169 364 EELEDLRAE-----LEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA---IAGIEA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 881 RVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEA 955
Cdd:TIGR02169 435 KINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE---LSKLQRELAEAEAQARASEER 505
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
544-922 |
2.55e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.91 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 544 AWGKPEEEQRGLQEAQLddtkvqegSQEEELRQANRELEKE---LQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSL 620
Cdd:PRK04863 273 DYMRHANERRVHLEEAL--------ELRRELYTSRRQLAAEqyrLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 621 ASLEAE---QASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------L 690
Cdd:PRK04863 345 RQQEKIeryQADLEELEERLEEQNEVVEEADE----QQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 691 RALESqCQQQTQL-----------IEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQ 749
Cdd:PRK04863 421 QALER-AKQLCGLpdltadnaedwLEEFQAKEQEA------TEELLSLEQKLSVAQAAHSQFEqayqlvrkiaGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 750 AQVVdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvQELLQCSEREGALQEERADEAQQREEE 829
Cdd:PRK04863 494 AWDV-----ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA------ERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 830 LRALQEELSQAKCSSEEAQLEHAELQEQL--------------HRANTDTAELGIQVCALTVEKERVEEALacavQELQD 895
Cdd:PRK04863 563 LEARLESLSESVSEARERRMALRQQLEQLqariqrlaarapawLAAQDALARLREQSGEEFEDSQDVTEYM----QQLLE 638
|
410 420
....*....|....*....|....*..
gi 1894925300 896 AKEAASREREGLERQVAGLQQEKESLQ 922
Cdd:PRK04863 639 RERELTVERDELAARKQALDEEIERLS 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
291-840 |
2.66e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 291 EDYHTALRRLE---SMLQPL---AQELEATRDSLDKKNQHLASFPGWlaMAQQKADTASDTKGRQEPIPSDAAQEMQELG 364
Cdd:COG4913 238 ERAHEALEDAReqiELLEPIrelAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 365 EKLQALERERTKVEEVNRQQS--------AQLEQLVKELQLKEDARASLERLVKEmapLQEELSGkgqEADQLWRRLQEL 436
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAA---LGLPLPA---SAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 437 LAHTSSWEEELAELRREkkqqqeekelleqeVRSLTRQLQFLETQLAQVSQHVSDLEEQKK----QLIQDKDHLSQQVGM 512
Cdd:COG4913 390 AALLEALEEELEALEEA--------------LAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 513 LERlagppgpELPVAGEkneaLVPVnsslqeawgKPEEEQ-RGLQEAQLddtkvqeGSQ-------EEELRQANReleke 584
Cdd:COG4913 456 DEA-------ELPFVGE----LIEV---------RPEEERwRGAIERVL-------GGFaltllvpPEHYAAALR----- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 585 lqnVVGRNQLlEGKLQALQAD-YQALQQRESAIQGSLAS-LEAEQASIR-----HLGDQM-------EASLLAVRKA--K 648
Cdd:COG4913 504 ---WVNRLHL-RGRLVYERVRtGLPDPERPRLDPDSLAGkLDFKPHPFRawleaELGRRFdyvcvdsPEELRRHPRAitR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 649 EAM---KAQMAEK----------------EAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTA 709
Cdd:COG4913 580 AGQvkgNGTRHEKddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 710 EKGQQGVgpptDNEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQ 789
Cdd:COG4913 660 EIDVASA----EREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 790 LKEQNEALNRAHVQELLQCSE--REGALQEERADEAQQR-EEELRALQEELSQA 840
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEerFAAALGDAVERELRENlEERIDALRARLNRA 785
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
817-1129 |
3.58e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 817 EERADEAQQREEELRALQEELsqakcsseEAQLEHAELQ-EQLHRANTDTAELGI-QVCALTVEKERVEEALACAVQELQ 894
Cdd:COG1196 178 ERKLEATEENLERLEDILGEL--------ERQLEPLERQaEKAERYRELKEELKElEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 895 DAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDY 974
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 975 QSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKE 1054
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 1055 LEKATTKIQEYYnklcQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1129
Cdd:COG1196 409 EEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| FYVE_RABE_unchar |
cd15739 |
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ... |
1127-1187 |
6.65e-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: 6.65e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 1127 EERWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRACF 1187
Cdd:cd15739 1 EVRWQHEDDVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVPSGPNRRPARVCDVCH 61
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
275-967 |
6.87e-12 |
|
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: 70.38 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 275 LQTCLQGLELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 354
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 355 DA-AQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElsgkgQEADQLWRRL 433
Cdd:TIGR00618 279 LEeTQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----RRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 434 QELLAhtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVS--QHVSDLEEQKKQLIQDKDHLSQQVG 511
Cdd:TIGR00618 354 EIHIR------------------------------DAHEVATSIREISCQQHTltQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 512 MLERLAGPPGPELpvageknEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKV-QEGSQEE----ELRQANRELEKELQ 586
Cdd:TIGR00618 404 ILQREQATIDTRT-------SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaQCEKLEKihlqESAQSLKEREQQLQ 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 587 NVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGdqmeasllAVRKAKEAMKAQMAEKEAILQSKE 666
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG--------PLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 667 GECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 746
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 747 RLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERAD----- 821
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtll 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 822 -EAQQREEELRALQEELSQAKcSSEEAQLEhAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ---ELQDAK 897
Cdd:TIGR00618 707 rELETHIEEYDREFNEIENAS-SSLGSDLA-AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLA 784
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 898 EAASREREGLERQVAGLQQEKESLQEKLkaaKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQL 967
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQEI---PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| RUN_RUFY1_like |
cd17681 |
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ... |
18-95 |
8.76e-12 |
|
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: 64.51 E-value: 8.76e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1894925300 18 KEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWY 95
Cdd:cd17681 50 KVKKSFLGPNKSFWPVLEHVEKLVPEANEITASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFY 127
|
|
| FYVE_PKHF |
cd15717 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ... |
1130-1187 |
9.90e-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: 9.90e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1130 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE-RCCRACF 1187
Cdd:cd15717 2 WVPDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKFLLPHQSSKPlRVCDTCY 61
|
|
| FYVE_RUFY4 |
cd15745 |
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ... |
1138-1187 |
1.03e-11 |
|
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: 60.98 E-value: 1.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 1138 HCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKH--GGKKERCCRACF 1187
Cdd:cd15745 1 ACAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVpdTCIYLRVCKTCY 52
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
194-994 |
1.35e-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: 69.60 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 194 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQA----TQ 269
Cdd:COG3096 310 EMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ-EKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEArleaAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 270 NTVKELQTCL----QGLELgAAEKEEDYHTALRRLESmlqplAQELeatrdsLDKKNQHLASFPGWLAMAQQKADTASDT 345
Cdd:COG3096 389 EEVDSLKSQLadyqQALDV-QQTRAIQYQQAVQALEK-----ARAL------CGLPDLTPENAEDYLAAFRAKEQQATEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 346 KGRQEPIPSDAAQEMQELGEKLQALERertKVEEVNRQQSAQLEQlvkelQLKEDARaSLERLVKEMAPLQEELSgkgqE 425
Cdd:COG3096 457 VLELEQKLSVADAARRQFEKAYELVCK---IAGEVERSQAWQTAR-----ELLRRYR-SQQALAQRLQQLRAQLA----E 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 426 ADQLWRRLQELlahtssweeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDH 505
Cdd:COG3096 524 LEQRLRQQQNA--------------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 506 LSQQVGMLERLAgppgpelPVAGEKNEALvpvnSSLQEAWGKPEEEQRGLQEA--QLDDTKVQEGSQEEELRQANRELEK 583
Cdd:COG3096 590 LRARIKELAARA-------PAWLAAQDAL----ERLREQSGEALADSQEVTAAmqQLLEREREATVERDELAARKQALES 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 584 ELQNVVGRNQLLEGKLQALQADYQALQQRE-------------SAIQGSLAS------LEAEQASIRHLGDQMEASLL-- 642
Cdd:COG3096 659 QIERLSQPGGAEDPRLLALAERLGGVLLSEiyddvtledapyfSALYGPARHaivvpdLSAVKEQLAGLEDCPEDLYLie 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 643 --------AVRKAKEAMKAQMA--EKEAILQSKEGEC------------QQLREEVEQcqqLAEaRHRELRALESQCQQQ 700
Cdd:COG3096 739 gdpdsfddSVFDAEELEDAVVVklSDRQWRYSRFPEVplfgraarekrlEELRAERDE---LAE-QYAKASFDVQKLQRL 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 701 TQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLqakmRAALDDQDKVQSQLS-MAEAV 779
Cdd:COG3096 815 HQAFSQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL----KEQLQLLNKLLPQANlLADET 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 780 LREhktLVQQLKEQNEALNRAhVQELLQCSEREGALqEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAEL----Q 855
Cdd:COG3096 891 LAD---RLEELREELDAAQEA-QAFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALsevvQ 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 856 EQLHRANTDTAELGIQVCALTvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSL 935
Cdd:COG3096 966 RRPHFSYEDAVGLLGENSDLN---EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEL 1042
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 936 PGLQAQL-AQAEQRAQSLQEAAHQELNTLKFQLS----------AEIMDYQSRLKNAGEECKSLRGQLEE 994
Cdd:COG3096 1043 EELGVQAdAEAEERARIRRDELHEELSQNRSRRSqlekqltrceAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
198-1064 |
2.14e-11 |
|
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: 69.05 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 198 ELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTC-----------LVAELQKQWEVTQ 266
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAArkqeleeilheLESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 267 ATQNTVKELQTCLQGLElGAAEKEEDYHTALR----RLESMLQPLAQELEATRDSLDKKN-------QHLASFPGWLAMA 335
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLE-EQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLEDQNSKLSkerklleERISEFTSNLAEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 336 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEevnrQQSAQLEQLVKELQLK-EDARASLERLVKEMAP 414
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLE----GESTDLQEQIAELQAQiAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 415 LQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQ-FLETQLAQV---SQHVS 490
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTAAQQelrSKREQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 491 DLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagEKNEALVPVNSSLqeawgkpeeEQRGLQEAQLDDTKVQEGSQ 570
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQ-------------KHTQALEELTEQL---------EQAKRNKANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 571 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 650
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 651 MKAQMAEKEAILQ-------SKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ-QTQLIEVLTAEKGQQGVGPPTDN 722
Cdd:pfam01576 466 LESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 723 EARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAhv 802
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE---KKQKKFDQMLAEEKAISARY-- 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 803 qellqCSEREGAlqeeradEAQQREEELRALQeeLSQAkcsSEEAQlehaELQEQLHRANTdtaELGIQVCALTVEKERV 882
Cdd:pfam01576 621 -----AEERDRA-------EAEAREKETRALS--LARA---LEEAL----EAKEELERTNK---QLRAEMEDLVSSKDDV 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 883 EEalacAVQELQDAKEAasreregLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQLAQAEQRAQSLQEAAHQELN 961
Cdd:pfam01576 677 GK----NVHELERSKRA-------LEQQVEEMKTQLEELEDELQATEDAKLRLEvNMQALKAQFERDLQARDEQGEEKRR 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 962 TLKFQ---LSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA----EEAVEKLKATQADMGEklsctsnHLAECQAAM 1034
Cdd:pfam01576 746 QLVKQvreLEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKD-------LQRELEEAR 818
|
890 900 910
....*....|....*....|....*....|
gi 1894925300 1035 LRKDKEGAALREDlERTQKELEKATTKIQE 1064
Cdd:pfam01576 819 ASRDEILAQSKES-EKKLKNLEAELLQLQE 847
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
827-1136 |
3.00e-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: 68.56 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 827 EEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERVEealacaVQELQDAKEAASREREG 906
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKEKREYE------GYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 907 LERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ-----AEQRAQSLQEAAHqELNTLKFQLSAEIMDYQSRLKNA 981
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 982 GEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTK 1061
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1062 IqeyyNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE-----FQQKLSAEERWLGDTEA 1136
Cdd:TIGR02169 401 I----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqLAADLSKYEQELYDLKE 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-847 |
3.20e-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: 68.54 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 186 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEVT 265
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---RLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 266 QATQNTVKELQtcLQGLELGAAEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDT 345
Cdd:TIGR02168 424 EELLKKLEEAE--LKELQAELEELEEELEELQEELER----LEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 346 KGRQEPIPSDAAQEMQE----------------------------LGEKLQAL------------------ERERTKVEE 379
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvvenlnaakkaiaflkqnELGRVTFLP 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 380 VNRQQSAQLEQLVKE-LQLKEDARASLERLVKEMAPLQEELSG---------KGQEADQLWRRLQ----------ELLAH 439
Cdd:TIGR02168 578 LDSIKGTEIQGNDREiLKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvdDLDNALELAKKLRpgyrivtldgDLVRP 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 440 TSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagp 519
Cdd:TIGR02168 658 GGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK---- 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 520 pgpELPVAGEKNEALVPVNSSLQEAWGKPEEeqrglQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKL 599
Cdd:TIGR02168 734 ---DLARLEAEVEQLEERIAQLSKELTELEA-----EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 600 QALQADYQALQQRESAIQGSLASLEAEQASIrhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 679
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 680 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAAQLALSQAQLEVHQGEVQRLQAQV-VDLQAK 758
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSE------LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLT 952
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 759 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnrahvqellqcseregALQEerADEAQQREEELRALQEELS 838
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA-----------------AIEE--YEELKERYDFLTAQKEDLT 1013
|
....*....
gi 1894925300 839 QAKCSSEEA 847
Cdd:TIGR02168 1014 EAKETLEEA 1022
|
|
| FYVE_RBNS5 |
cd15716 |
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ... |
1130-1191 |
3.48e-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: 3.48e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvlSKHGGKKERCCRACFQKLS 1191
Cdd:cd15716 4 WVNDSDVPFCPDCGKKFNLARRRHHCRLCGSIMCNKC------SQFLPLHIRCCHHCKDLLE 59
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
541-956 |
3.50e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 541 LQEAWGKPEEEQRGLQEAQLDDTKVQEGSQE-EELRQANRELEKELQN--VVGRNQLLEGKLQALQADYQALQQRESAIQ 617
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 618 GSLASLEAEQASIRHLGDQMEAsllAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQC 697
Cdd:COG4717 160 ELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 698 ---------QQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALS-------------QAQLEVHQGEVQRLQAQVVDL 755
Cdd:COG4717 237 eaaaleerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllarEKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 756 QAKMRAALDDQDKVQSQLS--MAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEaqqrEEELRAL 833
Cdd:COG4717 317 EEEELEELLAALGLPPDLSpeELLELLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAEAGVED----EEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 834 QEELSQAkcssEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEEALacavQELQDAKEAASREREGLERQVAG 913
Cdd:COG4717 391 LEQAEEY----QELKEELEELEEQLEELLGELEEL-----LEALDEEELEEEL----EELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1894925300 914 LQQEKESLQEKlkaakaaaGSLPGLQAQLAQAEQRAQSLQEAA 956
Cdd:COG4717 458 LEAELEQLEED--------GELAELLQELEELKAELRELAEEW 492
|
|
| FYVE_ZFYV1 |
cd15734 |
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ... |
1130-1187 |
4.22e-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: 4.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1187
Cdd:cd15734 2 WVPDSEIKECSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHpvRVCDPCA 61
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
744-1006 |
7.60e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 744 EVQRLQAQVVDLQAKMRAALDDQDKVQsQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQEllqcSEREGALQEERADEA 823
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLWF----AQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 824 qqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDT-AELGIQVCALTVEKERVEEALACAVQELQDAKEAASR 902
Cdd:COG4913 301 ---RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 903 EREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQelntlkfqLSAEIMDYQSRLKNAG 982
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEA----------LEEALAEAEAALRDLRRELRE--------LEAEIASLERRKSNIP 439
|
250 260
....*....|....*....|....
gi 1894925300 983 EECKSLRGQLEEqgrQLQAAEEAV 1006
Cdd:COG4913 440 ARLLALRDALAE---ALGLDEAEL 460
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
614-1057 |
1.02e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 614 SAIQGSLAS-LEAEQASIRHLGDQMEASLLAVRKAKEAMKaqmaekeaILQSKEGECQQLREEVEQCQQLAEARHRELRA 692
Cdd:PRK04863 211 SAITRSLRDyLLPENSGVRKAFQDMEAALRENRMTLEAIR--------VTQSDRDLFKHLITESTNYVAADYMRHANERR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 693 LESQcqqqtqliEVLTAEKGQQGvgpptdneARElaaQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQ 772
Cdd:PRK04863 283 VHLE--------EALELRRELYT--------SRR---QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 773 LSMAEAVLR---EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEERADEA-------QQREEEL--RALQEElsQA 840
Cdd:PRK04863 344 LRQQEKIERyqaDLEELEERLEEQNEV--VEEADEQQEENEARAEAAEEEVDELksqladyQQALDVQqtRAIQYQ--QA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 841 KCSSEEAQlehaelqEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLE--RQVAG----- 913
Cdd:PRK04863 420 VQALERAK-------QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvRKIAGevsrs 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 914 -LQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEIMDYQS 976
Cdd:PRK04863 493 eAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAerllaefckrlgknldDEDELEQLQEELEARLESLSE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 977 RLKNAGEECKSLRGQLEEQGRQLQ----------AAEEAVEKLkatQADMGEKLScTSNHLAECQAAMLRKDKEGAALRE 1046
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQrlaarapawlAAQDALARL---REQSGEEFE-DSQDVTEYMQQLLERERELTVERD 648
|
490
....*....|.
gi 1894925300 1047 DLERTQKELEK 1057
Cdd:PRK04863 649 ELAARKQALDE 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
469-1016 |
1.26e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 469 RSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQqvgMLERLAgppgpelpvagEKNEALVPVnsslqeawgkp 548
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE---VLEEHE-----------ERREELETL----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 549 EEEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLA----- 621
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEvrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrva 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 622 --SLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL----------AEARHRE 689
Cdd:PRK02224 337 aqAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapvdlgnAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 690 LRALESQCQQQTQLIEVlTAEKGQQGVgpptdNEARELAAQLALSQAQLEV----HQGEVQRLQAQVVDLQAKMRAALDD 765
Cdd:PRK02224 417 LREERDELREREAELEA-TLRTARERV-----EEAEALLEAGKCPECGQPVegspHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 766 QDKVQSQLSMAEAvLREHKTLVQQLKEQNEAlnrahVQELLqcseregALQEERADEAQQREEELRALQEEL-SQAKCSS 844
Cdd:PRK02224 491 VEEVEERLERAED-LVEAEDRIERLEERRED-----LEELI-------AERRETIEEKRERAEELRERAAELeAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 845 EEAQLEHAELQEQLHRAntdtAELGIQVCALTVEKERVEeALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEK 924
Cdd:PRK02224 558 EAAAEAEEEAEEAREEV----AELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 925 LKAAKAAAGSLPGLQAQLAQAE-QRAQSLQEAAHQELNTL---KFQLSAEIMDYQSRLKNAgEECKSLRGQLEEQGRQLQ 1000
Cdd:PRK02224 633 RERKRELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELreeRDDLQAEIGAVENELEEL-EELRERREALENRVEALE 711
|
570
....*....|....*.
gi 1894925300 1001 AAEEAVEKLKATQADM 1016
Cdd:PRK02224 712 ALYDEAEELESMYGDL 727
|
|
| FYVE_RUFY2 |
cd15759 |
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
1130-1186 |
1.65e-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: 1.65e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKERCCRAC 1186
Cdd:cd15759 4 WLKDKEATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSPKPVRVCDSC 60
|
|
| FYVE2_Vac1p_like |
cd15737 |
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ... |
1129-1163 |
1.76e-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: 1.76e-10
10 20 30
....*....|....*....|....*....|....*
gi 1894925300 1129 RWLGDTEANHCLDCKREFSWMVRRHHCRICGRIFC 1163
Cdd:cd15737 1 PWEDDSSVTHCPICLRSFGLLLRKHHCRLCGKVVC 35
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
523-1136 |
2.25e-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: 65.47 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 523 ELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANrELEKELQNVVGRNQLLEGKLQAL 602
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKE-ALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 603 QADYQALQQRESAIQGSLASLEAEqasIRHLGdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQL 682
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKK---IKDLG---EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 683 AEARHRELRALESQCQQQTQLIEVLTAE-KGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRA 761
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 762 ALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALN---RAHVQELLQCSE-REGALQEERADEAQQR--EEELRALQE 835
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAAdLSKYEQELYDLKEEYDrvEKELSKLQR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 836 ELSQAkcsseEAQLEHAELQEQLHRANTDTAELGIQ-VCALTVEKERVEEALACAVQ-----ELQ----DAKEAASRERE 905
Cdd:TIGR02169 491 ELAEA-----EAQARASEERVRGGRAVEEVLKASIQgVHGTVAQLGSVGERYATAIEvaagnRLNnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 906 GLERQVAGLQ--------QEKESLQEKLKAAKAAA--------------------------------------------- 932
Cdd:TIGR02169 566 LLKRRKAGRAtflplnkmRDERRDLSILSEDGVIGfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtle 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 933 ------------GSLPGLQAQLAQAEQRAQSLQEAAH-QELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 999
Cdd:TIGR02169 646 gelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1000 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT--------KIQEYYNKLCQ 1071
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripEIQAELSKLEE 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 1072 EVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALwqKSDALEFQQKLSAEERWLGDTEA 1136
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL--KEQIKSIEKEIENLNGKKEELEE 868
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
363-1010 |
2.41e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 363 LGEKLQALERERTKVEEVnRQQSAQLEQLVKElqlKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtss 442
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKF-IKRTENIEELIKE---KEKELEEVLREINEISSELPELREELEKLEKEVKELEEL------ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 443 weeelaelRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQliqdkdhlsqqvgmLERLAGPPGP 522
Cdd:PRK03918 237 --------KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------------LKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 523 ELPVAGEKNEALVPVNsSLQEAWGKPEEEQRGLQEaqlddtKVQEGSQEEELRQANRELEKELQNVVGRnqlLEGKLQAL 602
Cdd:PRK03918 295 YIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEE------RIKELEEKEERLEELKKKLKELEKRLEE---LEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 603 QaDYQALQQRESAIQGSLASLEAEQAsirhlgdqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEqcqql 682
Cdd:PRK03918 365 E-EAKAKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 683 aearhrELRALESQCQQQTQLIevltaekgqqgvgppTDNEARELaaqlalsqaqLEVHQGEVQRLQAQVVDLQAKMRAA 762
Cdd:PRK03918 430 ------ELKKAKGKCPVCGREL---------------TEEHRKEL----------LEEYTAELKRIEKELKEIEEKERKL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 763 LDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALNRAHVQELlqcsEREGALQEERADEAQQREEELRALQEELSQAK- 841
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEe 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 842 CSSEEAQLEHA--ELQEQLHRANTDTAELGIQvcalTVE--KERVEEaLACAVQELQDAKEAASREREGLERqvagLQQE 917
Cdd:PRK03918 554 LKKKLAELEKKldELEEELAELLKELEELGFE----SVEelEERLKE-LEPFYNEYLELKDAEKELEREEKE----LKKL 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 918 KESLQEKLKAAKAAAGSLPGLQAQLAQAEQRaqsLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGR 997
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKK---YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
650
....*....|...
gi 1894925300 998 QLQAAEEAVEKLK 1010
Cdd:PRK03918 702 ELEEREKAKKELE 714
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
722-1058 |
3.15e-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: 65.36 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 722 NEARELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRah 801
Cdd:COG3096 278 NERRELSERAL----ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIER-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 802 vqellqcseregalqeeradeaqqREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVC----ALTV 877
Cdd:COG3096 352 ------------------------YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqALDV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 878 EKER----------VEEALAC-------------------------------AVQELQDAKEAASREREGLE--RQVAG- 913
Cdd:COG3096 408 QQTRaiqyqqavqaLEKARALcglpdltpenaedylaafrakeqqateevleLEQKLSVADAARRQFEKAYElvCKIAGe 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 914 ------LQQEKESLqEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA----------------AHQELNTLKFQLSAEI 971
Cdd:COG3096 488 versqaWQTARELL-RRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAerlleefcqrigqqldAAEELEELLAELEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 972 MDYQSRLKNAGE---ECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAM---LRKDKEGAALR 1045
Cdd:COG3096 567 EELEEQAAEAVEqrsELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMqqlLEREREATVER 646
|
410
....*....|...
gi 1894925300 1046 EDLERTQKELEKA 1058
Cdd:COG3096 647 DELAARKQALESQ 659
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
571-1065 |
4.14e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 571 EEELRQANRELEKE----LQNVVGRNQLLEGKLQALQ---ADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEA--SL 641
Cdd:COG4717 48 LERLEKEADELFKPqgrkPELNLKELKELEEELKEAEekeEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 642 LAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEarhrELRALESQCQQQTQLIEVLTAEKGQQgvgppTD 721
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA----ELAELQEELEELLEQLSLATEEELQD-----LA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 722 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAlDDQDKVQSQLSMAEAVLRehkTLVQQLKEQNEALNRAH 801
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAA---LLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 802 VQELLQcseregALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtAELGIqvcALTVEKER 881
Cdd:COG4717 275 IAGVLF------LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-------AALGL---PPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 882 VEEALAcAVQELQDAKEAASREREglERQVAGLQQEKESLQEKLKAAKAaagslpglqAQLAQAEQRAQSLQEAAhQELN 961
Cdd:COG4717 339 LLELLD-RIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVEDE---------EELRAALEQAEEYQELK-EELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 962 TLKFQLSAEIMDYQSRLKNAGEEckSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSctsnhlaecqaaMLRKDKEG 1041
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELE------------QLEEDGEL 471
|
490 500
....*....|....*....|....
gi 1894925300 1042 AALREDLERTQKELEKATTKIQEY 1065
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAAL 495
|
|
| FYVE_PKHF2 |
cd15755 |
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ... |
1130-1190 |
4.46e-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: 4.46e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 1130 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1190
Cdd:cd15755 2 WVPDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSeKKFLLPSQSSKPVRVCDFCYDLL 64
|
|
| FYVE_ZFY26 |
cd15724 |
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ... |
1130-1188 |
5.53e-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: 56.37 E-value: 5.53e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 1130 WLGDTEANHCLDCKRE-FSWMVRRHHCRICGRIFCYYCCNNYVL-SKHGGKKERCCRACFQ 1188
Cdd:cd15724 1 WVPDEAVSVCMVCQVErFSMFNRRHHCRRCGRVVCSSCSTKKMLvEGYRENPVRVCDQCYE 61
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
352-1128 |
7.74e-10 |
|
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: 63.84 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 352 IPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLE--------RLVKEMAPLQEELSGKG 423
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkeklELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 424 QEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDK 503
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 504 DHLSQQVGMLERLagppgpelpvagEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEK 583
Cdd:pfam02463 317 KESEKEKKKAEKE------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 584 ELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR----------HLGDQMEASLLAVRKAKEAMKA 653
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILeeeeesielkQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 654 QMAEKEAILQSKEGECQQLREEVEQC--QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQL 731
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 732 ALSQAQLEVHQGEVQRLQAQVvdLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLvqqlkEQNEALNRAHVQELLQCSER 811
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQK--LVRALTELPLGARKLRLLIPKLKLPLKSIAVL-----EIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 812 EGALQEERADeaqQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQ 891
Cdd:pfam02463 618 DDKRAKVVEG---ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 892 ELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEI 971
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 972 MDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQAAMLRKDKEGAALREDLERT 1051
Cdd:pfam02463 775 ELAEEREKT---EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE------QLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1052 QKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEE 1128
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
|
| FYVE_FGD6 |
cd15743 |
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ... |
1130-1187 |
1.06e-09 |
|
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: 55.52 E-value: 1.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN-YVLSKHGGKKERCCRACF 1187
Cdd:cd15743 3 WIPDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNkAPLEYLKNKSARVCDECF 61
|
|
| FYVE_ANFY1 |
cd15728 |
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ... |
1127-1190 |
1.61e-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: 1.61e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 1127 EERWlgdTEANHCLDCKREFSWMVRRHHCRICGRIFCYYC-CNNYVLSKHG-GKKERCCRACFQKL 1190
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 ... |
1129-1190 |
1.86e-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: 1.86e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 1129 RWLGDTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACFQKL 1190
Cdd:cd15741 2 RWVRDNEVTMCMRCKEPFNALTrRRHHCRACGYVVCWKCSDYKAtLEYDGNKLNRVCKHCYVIL 65
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
471-1124 |
2.68e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 471 LTRQLQFLETQLAQVSQH---VSDLEEQKKQLIQDKDHLsqqvgmlerlagppgpelpvaGEKNEALVPVNSSLQEAWGK 547
Cdd:PRK04863 319 LNEAESDLEQDYQAASDHlnlVQTALRQQEKIERYQADL---------------------EELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 548 PEEEQRGLQEAQL--DDTK-----VQEGSQEEELR-----QANRELEK----------ELQNVVGRNQLLEGKLQALQAD 605
Cdd:PRK04863 378 QEENEARAEAAEEevDELKsqladYQQALDVQQTRaiqyqQAVQALERakqlcglpdlTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 606 YQALQQRESAIQGSLASLEAEQASIRHLGDQMEASlLAVRKAKEAmkaqmaekeailqskegeCQQLREEVEQCQQLaEA 685
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS-EAWDVAREL------------------LRRLREQRHLAEQL-QQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 686 RHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLalsQAQLEVHQGEvqrlQAQVVDLQAKMRAALDD 765
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL---EARLESLSES----VSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 766 QDKVQSQLSMAEAVLREHKTLVQQLKEQNEA--LNRAHVQELLQ-CSEREGALQEERaDEAQQREEELRALQEELSQAKC 842
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALARLREQSGEefEDSQDVTEYMQqLLERERELTVER-DELAARKQALDEEIERLSQPGG 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 843 SSEEAQLEHAE------LQE-----QLHRANTDTAELGIQVCALTV-EKERVEEALA----C------------------ 888
Cdd:PRK04863 670 SEDPRLNALAErfggvlLSEiyddvSLEDAPYFSALYGPARHAIVVpDLSDAAEQLAgledCpedlyliegdpdsfddsv 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 889 -AVQELQDA--KEAASRE-------------REGLERQVAGLQQEKESLQEKLkaakaaagslpglqAQLAQAEQRAQSL 952
Cdd:PRK04863 750 fSVEELEKAvvVKIADRQwrysrfpevplfgRAAREKRIEQLRAEREELAERY--------------ATLSFDVQKLQRL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 953 QEAAHQELNT---LKFQL--SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM--------GEK 1019
Cdd:PRK04863 816 HQAFSRFIGShlaVAFEAdpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1020 LSCTSNHLAECQAAMLRKDKEGAALR-------------EDLERTQKELEKATTKIQEYYNK---LCQEVTNRE----RN 1079
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAqlepivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQafaLTEVVQRRAhfsyED 975
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1080 DQKMLADLDDLN-RTKKYLEERLIELLRDKDALWQK----SDALEFQQKL 1124
Cdd:PRK04863 976 AAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAqaqlAQYNQVLASL 1025
|
|
| FYVE_WDFY3 |
cd15719 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ... |
1130-1190 |
2.83e-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: 2.83e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNN--YVLSKHGGKKERCCRACFQKL 1190
Cdd:cd15719 3 WVKDEGGDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFesEIRRLRISRPVRVCQACYNIL 65
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
556-1064 |
3.15e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 556 QEAQLDDTKVQ-EGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLg 634
Cdd:PRK02224 185 QRGSLDQLKAQiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 635 dqmEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVE---QCQQLAEARHRELRALESQCQQQTQLIEVLTAEK 711
Cdd:PRK02224 264 ---RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 712 GQQGVGPPTD------------NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAV 779
Cdd:PRK02224 341 NEEAESLREDaddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL---EEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 780 LREHKTLVQQLKE-----QNEALNRAHVQELL---QCSEREGALQE-ERADEAQQREEELRALQEELsqakcssEEAQLE 850
Cdd:PRK02224 418 REERDELREREAEleatlRTARERVEEAEALLeagKCPECGQPVEGsPHVETIEEDRERVEELEAEL-------EDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 851 HAELQEQLHRAnTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 930
Cdd:PRK02224 491 VEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 931 AAGSLPGLQAQLAQAEQRAQSLqeaahqelntlkfqlsAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1010
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESL----------------ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 1011 ATQADMGEKLSctsnhlaecqaamlrkDKEGAALREDLERTQKELEKATTKIQE 1064
Cdd:PRK02224 634 ERKRELEAEFD----------------EARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
550-916 |
4.03e-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: 61.51 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 550 EEQRGLQEAQLDDTKVQEGSQEE--ELRQANRELEKELQNVVGRNQLLEGKLQA----LQADYQALQQRESaiqgslasL 623
Cdd:COG3096 278 NERRELSERALELRRELFGARRQlaEEQYRLVEMARELEELSARESDLEQDYQAasdhLNLVQTALRQQEK--------I 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 624 EAEQASIRHLGDQMEASLLAVRKAKEamkaQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRE-------LRALEsQ 696
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAE----QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyqqaVQALE-K 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 697 CQQQTQLIEvLTAE-----------KGQQGvgpptDNEARELAAQLALSQAQLEVHQ----------GEVQRLQA----- 750
Cdd:COG3096 425 ARALCGLPD-LTPEnaedylaafraKEQQA-----TEEVLELEQKLSVADAARRQFEkayelvckiaGEVERSQAwqtar 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 751 QVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNR-------------AHVQELLQCSEREGALQE 817
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQqldaaeeleellaELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 818 ERAdEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELgIQVCALTVEKERveealacavqELQDAK 897
Cdd:COG3096 579 QRS-ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV-TAAMQQLLERER----------EATVER 646
|
410
....*....|....*....
gi 1894925300 898 EAASREREGLERQVAGLQQ 916
Cdd:COG3096 647 DELAARKQALESQIERLSQ 665
|
|
| FYVE_spVPS27p_like |
cd15735 |
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ... |
1134-1187 |
4.74e-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: 4.74e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 1134 TEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYVLSKHGGKKE--RCCRACF 1187
Cdd:cd15735 4 VDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQpvRVCDGCY 59
|
|
| FYVE_ZFY19 |
cd15749 |
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ... |
1139-1187 |
5.01e-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: 5.01e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1139 CLDCKREFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACF 1187
Cdd:cd15749 2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTfSAVVPRKGNQKQKVCKQCH 51
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
727-954 |
5.05e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 727 LAAQLALSQAQLEVHQGEVQRLQAQ--VVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNeALNRAHVQE 804
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL-GSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 805 LLQcSEREGALQEERADEAQQREEELRALQEELSQAKcsseeaqlehaELQEQLhrantdtaelgiqvcaltvekERVEE 884
Cdd:COG3206 259 LLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVI-----------ALRAQI---------------------AALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 885 ALAcavQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKaakaaagSLPGLQAQLAQAEQRAQSLQE 954
Cdd:COG3206 306 QLQ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLA-------ELPELEAELRRLEREVEVARE 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
680-924 |
1.02e-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: 59.01 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 680 QQLAEARHRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 759
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE-------------KALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 760 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcSEREGALQEERADEAQQREEELRALQEELSQ 839
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 840 AKcssEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 919
Cdd:COG4942 165 LR---AELEAERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 1894925300 920 SLQEK 924
Cdd:COG4942 238 AAAER 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
194-925 |
1.22e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 194 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQG--EQLQTERERGRTAAEDNVRLTCLVAELQKQWEV-TQATQN 270
Cdd:PRK04863 311 EMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkiERYQADLEELEERLEEQNEVVEEADEQQEENEArAEAAEE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 271 TVKELQTCL----QGLELgAAEKEEDYHTALRRLESM-----LQPLAQE-LEATRDSLDKKNQHLASFpgwLAMAQQKAD 340
Cdd:PRK04863 391 EVDELKSQLadyqQALDV-QQTRAIQYQQAVQALERAkqlcgLPDLTADnAEDWLEEFQAKEQEATEE---LLSLEQKLS 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 341 TASDTKGRQE-----------PI-PSDAAQEMQEL----------GEKLQALERERTKVEEVNRQQsAQLEQLVKEL--- 395
Cdd:PRK04863 467 VAQAAHSQFEqayqlvrkiagEVsRSEAWDVARELlrrlreqrhlAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFckr 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 396 ------------QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAelrrekkqqqeekel 463
Cdd:PRK04863 546 lgknlddedeleQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD--------------- 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 464 leqevrSLTR-QLQFLETQL--AQVSQHVSDLEEQKKQLIQDKDHLSQQVGML----ERLAGPPGPELPVAGEKNEALVP 536
Cdd:PRK04863 611 ------ALARlREQSGEEFEdsQDVTEYMQQLLERERELTVERDELAARKQALdeeiERLSQPGGSEDPRLNALAERFGG 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 537 VnsSLQEAWgkpeeeqrglqeaqlDDTKVQEGSQEE----ELRQA--NRELEKELQNVVGRNQLLEgKLQALQADYQALQ 610
Cdd:PRK04863 685 V--LLSEIY---------------DDVSLEDAPYFSalygPARHAivVPDLSDAAEQLAGLEDCPE-DLYLIEGDPDSFD 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 611 QresaiqGSLASLEAEQASIRHLGD-QMEAS------LLAvRKAKEAmkaQMAEKEAILQSKEGECQQLREEVEQCQQLA 683
Cdd:PRK04863 747 D------SVFSVEELEKAVVVKIADrQWRYSrfpevpLFG-RAAREK---RIEQLRAEREELAERYATLSFDVQKLQRLH 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 684 EA------------------------------RHRELRALESQCQQQTQLIEvlTAEKGQQGVG-----------PPTDN 722
Cdd:PRK04863 817 QAfsrfigshlavafeadpeaelrqlnrrrveLERALADHESQEQQQRSQLE--QAKEGLSALNrllprlnlladETLAD 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 723 EARELAAQLA-LSQAQLEVHQGevQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEalNRAH 801
Cdd:PRK04863 895 RVEEIREQLDeAEEAKRFVQQH--GNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQ--RRAH 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 802 ------VQELLQCSEREGALQEERADEAQQRE---EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQV 872
Cdd:PRK04863 971 fsyedaAEMLAKNSDLNEKLRQRLEQAEQERTrarEQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 873 CaltvekERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 925
Cdd:PRK04863 1051 D------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
194-858 |
1.43e-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: 59.60 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 194 EMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVK 273
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT-QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 274 ELQTCLQglELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLAsfpgwlAMAQQKADTASDTKgrqepip 353
Cdd:TIGR00618 281 ETQERIN--RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA------AHVKQQSSIEEQRR------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 354 sdAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEElSGKGQEADQLWRRL 433
Cdd:TIGR00618 346 --LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE-QATIDTRTSAFRDL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 434 QELLAHTSSWEEELAELRREKKQ----QQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQ 509
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 510 VGMLERLAGPPGPELPVAGEKNEALVPV---------------------NSSLQEAWGKPEEEQRGLQEAQLDDTKVQEG 568
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqletseedvyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 569 SQE--------EELRQANRELEKELQNVVGRNQLLEGKLQALQADYQA---LQQRESAIQGSLASLEAEQASIrhLGDQM 637
Cdd:TIGR00618 583 KEDipnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhLQQCSQELALKLTALHALQLTL--TQERV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 638 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLievltaekgqqgvg 717
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA-------------- 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 718 pptdneareLAAQLALSQAQLEVHQGEVQRLQAQvvdlqakMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAL 797
Cdd:TIGR00618 727 ---------SSSLGSDLAAREDALNQSLKELMHQ-------ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 798 NRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQL 858
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| FYVE_PKHF1 |
cd15754 |
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ... |
1130-1190 |
2.93e-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: 2.93e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 1130 WLGDTEANHCLDCKR-EFSWMVRRHHCRICGRIFCYYCCN-NYVLSKHGGKKERCCRACFQKL 1190
Cdd:cd15754 2 WIPDKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRqRFLIPRLSPKPVRVCSLCYRKL 64
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
539-1128 |
3.11e-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: 58.70 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 539 SSLQEAWGKPEEEQRGL--QEAQLDDTKVQEGSQEEELRQanrELEKELQNVVGRNQLLEGKLQALQADYQALQQ-RESA 615
Cdd:pfam12128 311 SAADAAVAKDRSELEALedQHGAFLDADIETAAADQEQLP---SWQSELENLEERLKALTGKHQDVTAKYNRRRSkIKEQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 616 IQGSLASLEAEQASIRhlgdqmeasllavrkakEAMKAQMAEKEAILQskeGECQQLREEVEQcqQLAEARhrelrales 695
Cdd:pfam12128 388 NNRDIAGIKDKLAKIR-----------------EARDRQLAVAEDDLQ---ALESELREQLEA--GKLEFN--------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 696 qcQQQTQLIEVLTAEKGQQGVGPPTDnearELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSM 775
Cdd:pfam12128 437 --EEEYRLKSRLGELKLRLNQATATP----ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 776 AEAVLREHKTLVQQLKEQNEAlnRAHvqELLQCSEREGALQEERADEAQQREEELRA-LQEELSQAKCSSEEA------- 847
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFP--QAG--TLLHFLRKEAPDWEQSIGKVISPELLHRTdLDPEVWDGSVGGELNlygvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 848 --QLEH---AELQEQLhRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLE-------RQVAGLQ 915
Cdd:pfam12128 587 lkRIDVpewAASEEEL-RERLDKAEEALQ--SAREKQAAAEEQLVQANGELEKASREETFARTALKnarldlrRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 916 QEKESLQEKlkaakaaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEImdyqsrlknageeckslRGQLEEQ 995
Cdd:pfam12128 664 SEKDKKNKA-------------LAERKDSANERLNSLEAQLKQLDKKHQ-AWLEEQ-----------------KEQKREA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 996 GRQLQAAEEAVEKLKATQADM--GEKLSCTSNHLAECQAAMLRKDKEGAAL-------------REDLERTQKELEKATT 1060
Cdd:pfam12128 713 RTEKQAYWQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDLASLgvdpdviaklkreIRTLERKIERIAVRRQ 792
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 1061 KIQEYYNKLcQEVTNRERndQKMLADLDDLNRTKKYLEERLIELL----RDKDALWQKSDALEFQQKLSAEE 1128
Cdd:pfam12128 793 EVLRYFDWY-QETWLQRR--PRLATQLSNIERAISELQQQLARLIadtkLRRAKLEMERKASEKQQVRLSEN 861
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
360-884 |
3.43e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 360 MQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAH 439
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 440 TSSWEEElaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLiqdkDHLSQQVGMLERlagp 519
Cdd:COG4717 128 LPLYQEL----------------------EALEAELAELPERLEELEERLEELRELEEEL----EELEAELAELQE---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 520 pgpelpvagEKNEALVPVNSSLQEAWGKPEEEQrglqeaqlddtkvqegsqeEELRQANRELEKELQNVVGRNQLLEGKL 599
Cdd:COG4717 178 ---------ELEELLEQLSLATEEELQDLAEEL-------------------EELQQRLAELEEELEEAQEELEELEEEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 600 QALQADYQALQQRES-AIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ 678
Cdd:COG4717 230 EQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 679 CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQL--ALSQAQLEVHQGEVQRLQAQVvdlQ 756
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE------ELQELLREAeeLEEELQLEELEQEIAALLAEA---G 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 757 AKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcsEREGALQEERADEAQQRE---EELRAL 833
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEelrEELAEL 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 834 QEELSQAKCSSE--EAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEE 884
Cdd:COG4717 459 EAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| FYVE_FGD5 |
cd15742 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ... |
1139-1190 |
3.88e-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: 3.88e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 1139 CLDCKREFSWMVRRHHCRICGRIFCYYCC-NNYVLSKHGGKKERCCRACFQKL 1190
Cdd:cd15742 12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSrNKYPLKYLKDRPAKVCDGCFAEL 64
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
727-992 |
4.35e-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: 57.08 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 727 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahvqELL 806
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 807 QCSEREGALQEERADEAQQREEELRALQEelsqakcSSEEAQLEHAELQEQLHRANTDTAELGiqvcALTVEKERVEEAL 886
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYR-------LGRQPPLALLLSPEDFLDAVRRLQYLK----YLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 887 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQEAAhQELNTLKFQ 966
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEA-EELEALIAR 231
|
250 260
....*....|....*....|....*.
gi 1894925300 967 LSAEIMDYQSRLKNAGEecKSLRGQL 992
Cdd:COG4942 232 LEAEAAAAAERTPAAGF--AALKGKL 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-925 |
4.59e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 179 DLNSPLNNEALEGFDEMRLELDQLEVREkqlrerMQQLDRENQ-----ELRAAVSQQGEQLQTERERGRTAAEDNVRLTC 253
Cdd:PTZ00121 1019 DFNQNFNIEKIEELTEYGNNDDVLKEKD------IIDEDIDGNhegkaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 254 LVAELQKQWEVTQATQNTVKELQTCLQglelgAAEKEEDYHTA--LRRLESmlqplAQELEATRDSLDKKNQHLASfpgw 331
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEE-----AKKKAEDARKAeeARKAED-----ARKAEEARKAEDAKRVEIAR---- 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 332 lamAQQKADTASDTKGRQEPIPSDAAQEMQELGEKlqaleRERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 411
Cdd:PTZ00121 1159 ---KAEDARKAEEARKAEDAKKAEAARKAEEVRKA-----EELRKAEDARKAEAARKAEEERKA---EEARKAEDAKKAE 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 412 MAPLQEELSGKGQEAdqlwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSD 491
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEA----KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 492 LEEQKKQLIQDK--DHLSQQVGMLERLAGPPGPELPVAGEKNEAlvpvnsSLQEAWGKPEEEQRGLQEAQLDDTKVQEGS 569
Cdd:PTZ00121 1304 ADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEA------AKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 570 QE--------EELRQANrELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQA----SIRHLGDQM 637
Cdd:PTZ00121 1378 KKadaakkkaEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadEAKKKAEEA 1456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 638 EASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEV----EQCQQLAEARHR--ELRALES--------QCQQQTQL 703
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkaDEAKKAAEAKKKadEAKKAEEakkadeakKAEEAKKA 1536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 704 IEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLR-- 781
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKae 1616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 782 EHKTLVQQLKEQNEAlnRAHVQELLQCSEREGALQEE----------RADEAQQREEELRALQEELSQA---KCSSEEAQ 848
Cdd:PTZ00121 1617 EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKKAEElkkaeeenkiKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 849 LEHAELQ---EQLHRANTDTAELGIQV-CALTVEKERVEEALACAVQELQDAKEAasREREGLERQVAGLQQEKESLQEK 924
Cdd:PTZ00121 1695 KKEAEEAkkaEELKKKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEE 1772
|
.
gi 1894925300 925 L 925
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 ... |
348-1050 |
4.71e-08 |
|
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: 57.88 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 348 RQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLK-------EDARASLERLVKEMAPLQEELS 420
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelcaeaEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 421 GKGQEADQLWRRLQ----ELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQK 496
Cdd:pfam01576 82 SRLEEEEERSQQLQnekkKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 497 KQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQE------AQLDDTKVQEGSQ 570
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiaelqAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 571 EEELRQANRELEKElqnvVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQasiRHLGDQMEasllAVRKAKEA 650
Cdd:pfam01576 242 EEELQAALARLEEE----TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR---RDLGEELE----ALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 651 MKAQMAEKEAILQSKEGECQQLREEVEQ-----CQQLAEARHRELRALESQCQQQTQLIEVLTA-EKGQQGVgpptDNEA 724
Cdd:pfam01576 311 TLDTTAAQQELRSKREQEVTELKKALEEetrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANlEKAKQAL----ESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 725 RELAAQL-ALSQAQLEVHQGEvQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQ 803
Cdd:pfam01576 387 AELQAELrTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 804 ELLQCSEREGALQEER------ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTV 877
Cdd:pfam01576 466 LESQLQDTQELLQEETrqklnlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 878 EKERVEEALACAVQELQDAKEAASReregLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ--AEQRAQSLQ-- 953
Cdd:pfam01576 546 GKKRLQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlAEEKAISARya 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 954 ------EAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEE-------QGRQLQAAEEAVEKLKATQADMGEKL 1020
Cdd:pfam01576 622 eerdraEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDlvsskddVGKNVHELERSKRALEQQVEEMKTQL 701
|
730 740 750
....*....|....*....|....*....|
gi 1894925300 1021 SCTSNHLAECQAAMLRKDKEGAALREDLER 1050
Cdd:pfam01576 702 EELEDELQATEDAKLRLEVNMQALKAQFER 731
|
|
| FYVE_scVPS27p_Vac1p_like |
cd15736 |
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ... |
1139-1187 |
6.30e-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: 6.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 1139 CLDCKREFSWMVRRHHCRICGRIFC-YYCCNNYVLSKHG-----GKKERCCRACF 1187
Cdd:cd15736 2 CHTCSRTFNLNIRAHHCRKCGKLFCrRHLPNMIPLNLSAydprnGKWYRCCHSCF 56
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
566-792 |
9.81e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 566 QEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQ--ALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 643
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 644 VRKAKEAMKAQMAE--KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEvltaekgqqgvgpptd 721
Cdd:COG3206 245 LRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------------- 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 722 neaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE 792
Cdd:COG3206 309 ---QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
333-1068 |
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 1894925300 333 AMAQQKAD-TASDTKGRQEPIPSDAAQEMQELGEKLQALER--ERTKVEEVNRQQSAQLEQLVKELQlkEDARASLERLV 409
Cdd:PTZ00121 1083 AKEDNRADeATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAE--DAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 410 KEMAplQEELSGKGQEAdqlwRRLQEllAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHV 489
Cdd:PTZ00121 1161 EDAR--KAEEARKAEDA----KKAEA--ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 490 SDL---EEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGE---KNEALVPVNSSLQEAWGKPEEEQRGLQEAQlddT 563
Cdd:PTZ00121 1233 EEAkkdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearKADELKKAEEKKKADEAKKAEEKKKADEAK---K 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 564 KVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLA 643
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 644 VRKAKEAMK--------AQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQtqliEVLTAEKGQQG 715
Cdd:PTZ00121 1390 KKKADEAKKkaeedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE----EAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 716 VGPPTDNEARELAAQLALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK---E 792
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeE 1544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 793 QNEALNRAHVQELLQCSEREGALQEERADE---------------AQQREEELRALQEELSQAKCSSEEAQLEHAELQEQ 857
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalrkaeeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 858 LHRANTDTAELGIQVCALTVEKERVEEAL----ACAVQELQDAKEAASREREGLERQVAglQQEKESLQEKLKAAKAAAG 933
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKkaeeENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 934 SLPGLQAQLAQAEQRAQSLQEAahQELNTLKfqlsaeimdyqsrlknaGEECKslRGQLEEQGRQLQAAEEAVEKLKATQ 1013
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKA--EEENKIK-----------------AEEAK--KEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 1014 ADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK 1068
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
473-849 |
1.22e-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: 56.88 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 473 RQLQFLETQLAQVSQHVSDLEEQKKQLIQD----KDHLS------QQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQ 542
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 543 EAwgkpeEEQRGLQEAQLDDTKVQEGSQEEEL----------RQANRELEKElQNVVGRNQL----LEGKLQALQADYQA 608
Cdd:COG3096 379 EA-----EARLEAAEEEVDSLKSQLADYQQALdvqqtraiqyQQAVQALEKA-RALCGLPDLtpenAEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 609 LQQRESAIQGSLASLEAEQAsirhlgdQMEASLLAVRKAKEAMKAQMAEKEAIlqskegecQQLREEVEQCQQLA----- 683
Cdd:COG3096 453 ATEEVLELEQKLSVADAARR-------QFEKAYELVCKIAGEVERSQAWQTAR--------ELLRRYRSQQALAQrlqql 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 684 EARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAAL 763
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQ----------LDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 764 DDQDKVQSQLSMAEAVLREHKTLVQQLKEQ-NEAL-NRAHVQELLQCS-EREGALQEERaDEAQQREEELRALQEELSQA 840
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALERLREQsGEALaDSQEVTAAMQQLlEREREATVER-DELAARKQALESQIERLSQP 666
|
....*....
gi 1894925300 841 KcSSEEAQL 849
Cdd:COG3096 667 G-GAEDPRL 674
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
820-1059 |
1.59e-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: 55.16 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 820 ADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcaltvekerveeALACAVQELQDAKEA 899
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------------------ALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 900 ASREREGLERQVAGLQQEKESLQEKLKA---AKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQS 976
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 977 RLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1056
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1894925300 1057 KAT 1059
Cdd:COG4942 241 ERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-650 |
1.88e-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: 55.16 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 396 QLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELlahtssweeelaelrrekkqqqeekellEQEVRSLTRQL 475
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----------------------------ERRIAALARRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 476 QFLETQLAQVSQHVSDLEEQ----KKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEALVPVNSSLQEAwgkpeEE 551
Cdd:COG4942 72 RALEQELAALEAELAELEKEiaelRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-----AP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 552 QRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIR 631
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*....
gi 1894925300 632 HLGDQMEASLLAVRKAKEA 650
Cdd:COG4942 227 ALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
276-923 |
2.29e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 276 QTCLQGLELGAAEKEE-DYHTALRRLEsmlqplaQELEATRDSLDKKNqhlasfpgwlamaqQKADTASDTKGRQEPIPS 354
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEkDLHERLNGLE-------SELAELDEEIERYE--------------EQREQARETRDEADEVLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 355 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLvkelqlkEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQ 434
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEV-------RDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 435 EllahtssweeelaelrrekkqqqeekelleqevrsLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQvgmle 514
Cdd:PRK02224 318 E-----------------------------------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 515 rlagppgpelpvAGEKnealvpvnsslqeawgkpeEEQRGLQEAQLDDTKVQEGSQEEELrqanRELEKELQNVVGRNQL 594
Cdd:PRK02224 358 ------------AEEL-------------------REEAAELESELEEAREAVEDRREEI----EELEEEIEELRERFGD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 595 LEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgdqmeasllAVRKAKEAMKAqmaekeailqSKEGECQQLRE 674
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARE----------RVEEAEALLEA----------GKCPECGQPVE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 675 EVEQCQQLAEARHR------ELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRL 748
Cdd:PRK02224 463 GSPHVETIEEDRERveeleaELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 749 QAQVVDLQAKMRAALDDQDKVQSQlsmAEAVLREHKTLVQQLKEQNEALNR-AHVQELL----QCSEREGALQEERADEA 823
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEE---AEEAREEVAELNSKLAELKERIESlERIRTLLaaiaDAEDEIERLREKREALA 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 824 Q---QREEELRALQEELSQAKCSSEEAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAA 900
Cdd:PRK02224 620 ElndERRERLAEKRERKRELEAEFDEARIE--EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697
|
650 660
....*....|....*....|....*.
gi 1894925300 901 SReREGLERQVAGLQ---QEKESLQE 923
Cdd:PRK02224 698 ER-REALENRVEALEalyDEAEELES 722
|
|
| FYVE_MTMR_unchar |
cd15738 |
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ... |
1130-1187 |
2.40e-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: 2.40e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1130 WLGDTEANHClDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKH-GGKKERCCRACF 1187
Cdd:cd15738 3 WKSFRNVTEC-SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRaLPGHlSQRPVPVCRACY 61
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
550-762 |
2.47e-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: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 550 EEQRGLQEAQLDDTKVQEGSQEEELRQANREL---EKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAE 626
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 627 QASIRHLG-----------DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALES 695
Cdd:COG4942 113 LYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 696 QCQQQTQLIevltaekgqqgvgpptdneaRELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAA 762
Cdd:COG4942 193 LKAERQKLL--------------------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
809-1127 |
2.60e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 809 SEREGALQEERADEAQQREEELRALQEELSQaKCSSEEAQLEHAELQEQLHRANTDTAELgiqvcALTVEKERVEE--AL 886
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLES-ELAELDEEIERYEEQREQARETRDEADE-----VLEEHEERREEleTL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 887 ACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG----SLPGLQAQLAQAEQRAQSLQE------AA 956
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRDrleecrVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 957 HQELNTLKFQLSAEIMDYQSRLKNAGEECKSL-------RGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAE 1029
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELeseleeaREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1030 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLC-QEVTNRERNDQkmladLDDLNRTKKYLEERLIELLRDK 1108
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKCPECgQPVEGSPHVET-----IEEDRERVEELEAELEDLEEEV 491
|
330
....*....|....*....
gi 1894925300 1109 DALWQKSDALEFQQKLSAE 1127
Cdd:PRK02224 492 EEVEERLERAEDLVEAEDR 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-557 |
2.67e-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: 55.46 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 201 QLEVREKQLRERMQQLDRENQELRAAVSQQgEQLQTERERGRTAAEDNVRltclvaELQKQWEVTQATQNTVKELQTclq 280
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIG------EIEKEIEQLEQEEEKLKERLE--- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 281 glelgaaekeedyhtalrRLESMLQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASDTKGRQEPIPSDAAQEM 360
Cdd:TIGR02169 741 ------------------ELEEDLSSLEQEIENVKSELKELEARI---------EELEEDLHKLEEALNDLEARLSHSRI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 361 QELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEmapLQEELSGKGQEADQLWRRLQELLAHT 440
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 441 SSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlagPP 520
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE----EI 946
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 521 GPELPVAG----------EKNEALVPVN--------------SSLQEAWGKPEEEQRGLQE 557
Cdd:TIGR02169 947 PEEELSLEdvqaelqrveEEIRALEPVNmlaiqeyeevlkrlDELKEKRAKLEEERKAILE 1007
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
211-1103 |
2.74e-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: 55.44 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 211 ERMQQLdreNQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLE--LGAAE 288
Cdd:TIGR00606 189 ETLRQV---RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 289 KEEDYHTALRRLESMLQPLAQELEATRDSL----DKKNQHLASFPGwlAMAQQKADTASDTKGRQEPIpsdaAQEMQELG 364
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQ--RTVREKERELVDCQRELEKL----NKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 365 EKLQALERERTKVE---EVNRQQSAQLEQLVKELQLKEDAR-----ASLERLVKEMAPL-QEELSGKGQEADQLWRRLQE 435
Cdd:TIGR00606 340 QEKTELLVEQGRLQlqaDRHQEHIRARDSLIQSLATRLELDgfergPFSERQIKNFHTLvIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 436 LLAHTsswEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSqqvgMLER 515
Cdd:TIGR00606 420 KERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS----KAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 516 LAGPPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVG---RN 592
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 593 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR-KAKEAMKAQmaekeailqSKEGECQQ 671
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdKLFDVCGSQ---------DEESDLER 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 672 LREEVEQCQQ----LAEARH------RELRALESQC--------QQQTQLIEVLTAEKGQQGVGP----PTDNEARELAA 729
Cdd:TIGR00606 644 LKEEIEKSSKqramLAGATAvysqfiTQLTDENQSCcpvcqrvfQTEAELQEFISDLQSKLRLAPdklkSTESELKKKEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 730 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEA-------------VLREHKTLVQQLKEQNEA 796
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtimpeeesakVCLTDVTIMERFQMELKD 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 797 LNRAHVQEL--LQCSEREGALQEERaDEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCA 874
Cdd:TIGR00606 804 VERKIAQQAakLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 875 LTVEKERVEEaLACAVQELQDAKEAASREREGLERQVAGLQQEKESLQeklkaakaaagslpglqaqlaqaeQRAQSLQE 954
Cdd:TIGR00606 883 RQQFEEQLVE-LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELI------------------------SSKETSNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 955 AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAA-EEAVEKLKATQADMGE-KLSCTSNHLAEC-- 1030
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKHQEKINEDMRLmRQDIDTQKIQERwl 1017
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 1031 --QAAMLRKDKEGAALREDLERTQKEL-EKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1103
Cdd:TIGR00606 1018 qdNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
899-1137 |
2.77e-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: 54.38 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 899 AASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSlpgLQAQLAQAEQRAQSLQEAAhQELNTLKFQLSAEIMDYQSRL 978
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 979 KNAGEECKSLRGQLEEQGRQLQAAEEAVE-KLKATQAD------MGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERT 1051
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1052 QKELEKATTKIQEYYNKLCQEVTNRERNdqkmladLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEERWL 1131
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKL-------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
....*.
gi 1894925300 1132 GDTEAN 1137
Cdd:COG4942 246 AGFAAL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
744-1126 |
3.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 744 EVQRLQAQVVDLQAKM---RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEAlnRAHVQELLQCsEREGALQEERA 820
Cdd:COG4717 72 ELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQL--LPLYQELEAL-EAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 821 DEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALAcAVQELQDAKEAA 900
Cdd:COG4717 149 EELEERLEELRELEEEL-------EELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQ-RLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 901 SREREGLERQVAGLQQEKESLQEK------------------LKAAKAAAGSLP-----------GLQAQLAQAEQRAQS 951
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLIltiagvlflvlGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 952 LQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNH--LAE 1029
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1030 CQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtnRERNDQKMLADLDDLNRTKKYLEERLIELLRDKD 1109
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELA 456
|
410
....*....|....*..
gi 1894925300 1110 ALWQKSDALEFQQKLSA 1126
Cdd:COG4717 457 ELEAELEQLEEDGELAE 473
|
|
| RUN_RUNDC3 |
cd17684 |
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ... |
30-95 |
3.94e-07 |
|
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: 50.86 E-value: 3.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 30 YWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWY 95
Cdd:cd17684 59 FWDYIRVACKKV--PQNCIASIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFY 122
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
650-901 |
7.30e-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: 53.23 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 650 AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQqgvgppTDNEARELAA 729
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 730 QLALSQAQLEVHQGEVQRL--QAQVVDLQAKMRAALDDQDKVQSQ--LSMAEAVLREHKTLVQQLKEQNEALNRAHvqel 805
Cdd:COG4942 91 EIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALR---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 806 lqcseregALQEERADEAQQREEELRALQEELSQAKcsseeaqlehAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 885
Cdd:COG4942 167 --------AELEAERAELEALLAELEEERAALEALK----------AERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*.
gi 1894925300 886 LACAVQELQDAKEAAS 901
Cdd:COG4942 229 IARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
598-847 |
8.04e-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: 53.23 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 598 KLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQskegecqQLREEVE 677
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 678 QCQQLAEARHRELRALESQCQ---QQTQLIEVLTAEkgqqgvgpptdnEARELAAQLALSQAQLEVHQGEVQRLQAQVVD 754
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYrlgRQPPLALLLSPE------------DFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 755 LQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvqellqcsEREGALQEERADEAQQREEELRALQ 834
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARL---------EKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 1894925300 835 EELSQAKCSSEEA 847
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
475-831 |
9.40e-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: 53.80 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 475 LQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpeLPVAGEKNEAlvpvnsSLQEAWGKPEEEQRG 554
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL-------LPQANLLADE------TLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 555 LQEAQLddtkvqegsqeeELRQANRELEkELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLG 634
Cdd:COG3096 905 AQEAQA------------FIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFS 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 635 DQMEASLLAVRKA-KEAMKAQMAEKEAilqskegECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQ 713
Cdd:COG3096 972 YEDAVGLLGENSDlNEKLRARLEQAEE-------ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 714 QGVGPPTDNEAR------ELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlreHKTLV 787
Cdd:COG3096 1045 LGVQADAEAEERarirrdELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA----GWCAV 1120
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 788 QQLKEQNEALNRAHVQELLQCSERE---------GALQEERADeaqqrEEELR 831
Cdd:COG3096 1121 LRLARDNDVERRLHRRELAYLSADElrsmsdkalGALRLAVAD-----NEHLR 1168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
773-1119 |
9.62e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 773 LSMAEAVLREHKTLVQQ---LKEQNEALNRAhvqellqcseregalQEERADEAQQREEELRALQEELSQAKCSSEEAQL 849
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQiseLKKQNNQLKDN---------------IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 850 EHAELQEQLHRANTDTAELGIQVCALTVE-----KERVEEALACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEK 924
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEK----KLEEIQNQISQNNKIISQLNEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 925 LKAAKAAAGSLPG----LQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQ 1000
Cdd:TIGR04523 344 ISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1001 AAEEAVEKLKATQADMGEKLSCTSNhlaecqaamlrKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERND 1080
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTN-----------QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350
....*....|....*....|....*....|....*....
gi 1894925300 1081 QKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALE 1119
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
|
| FYVE1_Vac1p_like |
cd15761 |
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ... |
1130-1198 |
9.70e-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: 9.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 1130 WLGDTEANHCLDCKREFSWMVRRHHCRICGRIFCYYCCNNYV-LSKHG------GKKERCCRACFqklSEGPGSPD 1198
Cdd:cd15761 4 WKKPSGKSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRNRIkLNNSAeydpknGKWCRCCEKCF---TSRPGYND 76
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
539-1071 |
1.10e-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: 53.19 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 539 SSLQEAWGKPEEEQRGLQEAQLDDTKV----QEGSQE--------------------------EELRQANRELEKELQNV 588
Cdd:pfam05483 106 NKLQENRKIIEAQRKAIQELQFENEKVslklEEEIQEnkdlikennatrhlcnllketcarsaEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 589 VGRNQLLEGKLQALQadyQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEA-------I 661
Cdd:pfam05483 186 MDLNNNIEKMILAFE---ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENkmkdltfL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 662 LQSKEGECQQLREEV----EQCQQLAEARHRELRALES-QCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQA 736
Cdd:pfam05483 263 LEESRDKANQLEEKTklqdENLKELIEKKDHLTKELEDiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 737 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKE--QNEALNRAHVQELLqcSEREGA 814
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfkNNKEVELEELKKIL--AEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 815 LQEERADEA----------------QQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVE 878
Cdd:pfam05483 421 LDEKKQFEKiaeelkgkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 879 KERVEEALACAVQELQDAKE---AASREREGLERQVAGLQQEKESLQEKLKAAKAA-AGSLPGLQAQLAQAEQRAQSLQE 954
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEdiiNCKKQEERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEY 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 955 AAHQELNTLKF------QLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL-SCTSNHL 1027
Cdd:pfam05483 581 EVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFeEIIDNYQ 660
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1894925300 1028 AECQAAMLRKDKegaaLREDLERTQKELEKAtTKIQEYYNKLCQ 1071
Cdd:pfam05483 661 KEIEDKKISEEK----LLEEVEKAKAIADEA-VKLQKEIDKRCQ 699
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
608-1129 |
1.13e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 608 ALQQRESAIQGSLASLEAEQASIRH-LG-DQMEASLLAVRKAKEAMKAQMAEKEAILQSKEgECQQLREEVEQcqQLAEA 685
Cdd:PRK03918 129 AIYIRQGEIDAILESDESREKVVRQiLGlDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE-NIEELIKEKEK--ELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 686 RhRELRALESQCQQQTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQ---AKMRAA 762
Cdd:PRK03918 206 L-REINEISSELPELREELEKLEKEV----------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEeriEELKKE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 763 LDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRahVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKC 842
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE--IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 843 SSEEAQLEHAELQE---QLHRANTDTAELGIQvcaltvEKERVEEALacavQELQDAKEAASREREGLERQVAGLQQEKE 919
Cdd:PRK03918 353 RLEELEERHELYEEakaKKEELERLKKRLTGL------TPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 920 SLQEKLKAAKAAAGSLPGLQAQLAqaEQRAQSLQEAAHQELNtlkfQLSAEIMDYQSRLKNAGEECKSLRGQLEEQgRQL 999
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGRELT--EEHRKELLEEYTAELK----RIEKELKEIEEKERKLRKELRELEKVLKKE-SEL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1000 QAAEEAVEKLKATQadmgEKLSCTSnhlaecqaamlrkdkegaalREDLERTQKELEKattkIQEYYNKLCQEVTNRERN 1079
Cdd:PRK03918 496 IKLKELAEQLKELE----EKLKKYN--------------------LEELEKKAEEYEK----LKEKLIKLKGEIKSLKKE 547
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1080 dqkmLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1129
Cdd:PRK03918 548 ----LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
474-700 |
1.14e-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: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 474 QLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpelpvagekneALVPVNSSLQEAwgkpeEEQR 553
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------------RIAALARRIRAL-----EQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 554 GLQEAQLDDTKVQEGSQEEELRQANRELEKELQNV--VGRNQLLEG------------KLQALQADYQALQQRESAIQGS 619
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALyrLGRQPPLALllspedfldavrRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 620 LASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQ 699
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1894925300 700 Q 700
Cdd:COG4942 239 A 239
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
571-925 |
1.19e-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: 52.98 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 571 EEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEA 650
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 651 MKAqmaEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQT-QLIEVLTAEKGQQGVGPPTDNEARE 726
Cdd:pfam07888 113 LSE---EKDALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKERAKKAGaQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 727 LAAQLALSQAQLEVHQGEVQRLQAQVVDLQ----------AKMRAALDDQDKVQSQLSM----AEAVLREHKTLVQQLKE 792
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttahrkeAENEALLEELRSLQERLNAserkVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 793 QNEALNRAHVQEL---LQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG 869
Cdd:pfam07888 270 TQAELHQARLQAAqltLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 870 IQV-CALTVEKERVEEalacaVQELQDAKEAASREREGLERQVAGLQQEKESLQEKL 925
Cdd:pfam07888 350 REKdCNRVQLSESRRE-----LQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
363-766 |
1.53e-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: 52.59 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 363 LGEKLQALERERTkveEVNRQQSAQLEQLVKELQLKEDARASLERLVKEM----APLQEELSGKGQEADQLWRRLQELLA 438
Cdd:pfam07888 32 LQNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELesrvAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 439 HTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLErlag 518
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE---- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 519 ppgpelpvageknEALVPVNSSLQEAwgKPEEEQRGLQEAQLDDTKVQegsqeeelrqanrelekeLQNVVGRNQLLEGK 598
Cdd:pfam07888 185 -------------EELRSLSKEFQEL--RNSLAQRDTQVLQLQDTITT------------------LTQKLTTAHRKEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 599 LQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAekEAILQSKEGECQQLREEvEQ 678
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA--DASLALREGRARWAQER-ET 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 679 CQQLAEARH-------RELRALESQCQQQTQLIEVLTAEKGQQ-----GVGPPTDNEARELAAQLALSQAQLEVHQGEVQ 746
Cdd:pfam07888 309 LQQSAEADKdrieklsAELQRLEERLQEERMEREKLEVELGREkdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQ 388
|
410 420
....*....|....*....|
gi 1894925300 747 RLQAQVVDLQAKMRAALDDQ 766
Cdd:pfam07888 389 ELLEYIRQLEQRLETVADAK 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
641-1121 |
1.65e-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: 53.05 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 641 LLAVRKAKEAMKAQMAEKEAILQSKEGecqqlREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgppt 720
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEKKELLMNLFP-----LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDT------ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 721 dneARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRA 800
Cdd:TIGR00618 217 ---YHERKQVLEKELKHLREALQQTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 801 --------HVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQv 872
Cdd:TIGR00618 290 rkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 873 caltvEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLaQAEQRAQSL 952
Cdd:TIGR00618 369 -----EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 953 QEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC-- 1030
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdn 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1031 ----QAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNK---LCQEVTNRERNDQKMLADLDDLNRTKKYLEERLIE 1103
Cdd:TIGR00618 523 pgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
490
....*....|....*...
gi 1894925300 1104 LLRDKDALWQKSDALEFQ 1121
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRK 620
|
|
| FYVE_WDFY1_like |
cd15718 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ... |
1134-1187 |
2.39e-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: 46.55 E-value: 2.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1134 TEANHCLDCKREFSW----M-------VRRHHCRICGRIFCYYCCNNY-VLSKHGGKKE-RCCRACF 1187
Cdd:cd15718 4 AESDNCQKCSRPFFWnfkqMwekktlgVRQHHCRKCGKAVCDKCSSNRsTIPVMGFEFPvRVCNECY 70
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
196-693 |
3.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 196 RLELDQLEVREKQLRERMQQLDrENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAELQKQWEVTQATQNTVKEL 275
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 276 QTCLQGLElgaaEKEEDYHTALRRLESmlqpLAQELEATRDSLDKKNQHLaSFPGWLAMaqqkadtasdtkgrqepipSD 355
Cdd:COG4717 145 PERLEELE----ERLEELRELEEELEE----LEAELAELQEELEELLEQL-SLATEEEL-------------------QD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 356 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARaslerlvkemaplqeelsgKGQEADQLWRRLQE 435
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-------------------RLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 436 LLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLsqqvgmler 515
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 516 lagppGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQRGLQEAQLddtkvqEGSQEEELRQANRELEKELQNVVGRNQLL 595
Cdd:COG4717 329 -----GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL------EQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 596 EGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQ--SKEGECQQLR 673
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELAELEAELEqlEEDGELAELL 475
|
490 500
....*....|....*....|
gi 1894925300 674 EEVEQCQQLAEARHRELRAL 693
Cdd:COG4717 476 QELEELKAELRELAEEWAAL 495
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
186-639 |
4.12e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 186 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgRTAAEDNVRLTCLVAE--LQKQWE 263
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-RDDLLAEAGLDDADAEavEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 264 VTQATQNTVKELQTCLQGLEL------GAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQ 337
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAhneeaeSLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 338 KADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLE--------QLVKE---LQLKEDARASLE 406
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGsphVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 407 RLVKEMAPLQEELSGKGQEADQLwRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQ-- 484
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEkr 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 485 ------------VSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGpPGPELPVAGEKNEALVPVNSSLQEAWGKPEEEQ 552
Cdd:PRK02224 558 eaaaeaeeeaeeAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKRERK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 553 RGLqEAQLDDTKVqegsqeEELRQANRELEKELQNVvgrnqllEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRH 632
Cdd:PRK02224 637 REL-EAEFDEARI------EEAREDKERAEEYLEQV-------EEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
....*..
gi 1894925300 633 LGDQMEA 639
Cdd:PRK02224 703 LENRVEA 709
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
723-855 |
4.14e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 50.43 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 723 EARELAAQLALSQAQLEVHQGEVQRLQAQVvDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHV 802
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEAEL-GAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARA 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 803 QELLQCSEREGALQEERADEAQQRE-EELRALQEELSQAkcsseEAQLEHAELQ 855
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQAGLREeEELAAAQAQVAQA-----EAALAQAELN 204
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
722-959 |
4.44e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 722 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREH----------KTLVQQL- 790
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDVLl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 791 --KEQNEALNRAHVQELLQcseregALQEERADEAQQREEELRALQEELSQAKcssEEAQLEHAELQEQLHRANTDTAEL 868
Cdd:COG3883 110 gsESFSDFLDRLSALSKIA------DADADLLEELKADKAELEAKKAELEAKL---AELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 869 GIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR 948
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
250
....*....|.
gi 1894925300 949 AQSLQEAAHQE 959
Cdd:COG3883 261 SAGAAGAAAGA 271
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
569-1119 |
4.56e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 569 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQ---QRESAIQGSLASLEAEQASIRHLGDQMEASLLAVR 645
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 646 KAKEAMKAQMAEkeaiLQSKEGECQQLREEVEqcqqlaeaRHRELRALESQCQQQTQLIEVLTAEkgqqgvgppTDNEAR 725
Cdd:PRK03918 266 ERIEELKKEIEE----LEEKVKELKELKEKAE--------EYIKLSEFYEEYLDELREIEKRLSR---------LEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 726 ELAAQLAlsqaQLEVHQGEVQRLQAQVVDLQAKMrAALDDQDKVQSQLSMAEAVLREHKTlvqqlKEQNEALNRAhVQEL 805
Cdd:PRK03918 325 GIEERIK----ELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKK-----RLTGLTPEKL-EKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 806 LQCSEREGALQEE------RADEAQQREEELRALQEELSQAK-----CSSEEAQLEHAELQE----QLHRANTDTAELGI 870
Cdd:PRK03918 394 EELEKAKEEIEEEiskitaRIGELKKEIKELKKAIEELKKAKgkcpvCGRELTEEHRKELLEeytaELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 871 QVCALTVEKERVEEALAcAVQELQDAKEAASREREgLERQVAGLQQEKesLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQ 950
Cdd:PRK03918 474 KERKLRKELRELEKVLK-KESELIKLKELAEQLKE-LEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 951 SLQEaahqelntlkfqLSAEIMDYQSRLKNAGEECKSLRGQLEEQGrqLQAAEEAVEKLKATQADMGEKLScTSNHLAEC 1030
Cdd:PRK03918 550 KLEE------------LKKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKELEPFYNEYLE-LKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1031 QAAMLRKDKEGAAL---REDLERTQKELEKATTKI--------QEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE 1099
Cdd:PRK03918 615 EREEKELKKLEEELdkaFEELAETEKRLEELRKELeelekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
570 580
....*....|....*....|
gi 1894925300 1100 RLIELLRDKDALWQKSDALE 1119
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELE 714
|
|
| RUN |
pfam02759 |
RUN domain; This domain is present in several proteins that are linked to the functions of ... |
18-124 |
5.61e-06 |
|
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: 47.27 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 18 KEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRT---SLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDW 94
Cdd:pfam02759 21 ILRAAGLLPERSFWALLERVGKLVPPAEELLSSVQELEQIHTpysPDGRGRAWIRLALNEKLLDQWLKLLLSNKELLSEY 100
|
90 100 110
....*....|....*....|....*....|
gi 1894925300 95 YYARSPFLQPKLSSDIVGQLYELTEVQFDL 124
Cdd:pfam02759 101 YEPWALLADPEFGEILLGLLVGLSALDFNL 130
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
570-1060 |
7.56e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.57 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 570 QEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAiQGSLASLEAEQ--ASIRHLGD---QMEASLLAV 644
Cdd:PRK10246 231 EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-QPQLAALSLAQpaRQLRPHWEriqEQSAALAHT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 645 RKAKEAMKAQMAEKEA----ILQSKEGECQQLREEVEQCQQ-LAEAR-----HREL---RALESQC----QQQTQLIEVL 707
Cdd:PRK10246 310 RQQIEEVNTRLQSTMAlrarIRHHAAKQSAELQAQQQSLNTwLAEHDrfrqwNNELagwRAQFSQQtsdrEQLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 708 TAEKGQQGVGPPT--DNEARELAAQLALSQAQLEVHQgEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKt 785
Cdd:PRK10246 390 THAEQKLNALPAItlTLTADEVAAALAQHAEQRPLRQ-RLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMR- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 786 lvQQLKEQNEALNRahVQELLQCSEREGALQEERA---------------------------DEAQQR----EEELRALQ 834
Cdd:PRK10246 468 --QRYKEKTQQLAD--VKTICEQEARIKDLEAQRAqlqagqpcplcgstshpaveayqalepGVNQSRldalEKEVKKLG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 835 EELSQAKcsseeAQLEhaELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAK----EAASRERE----- 905
Cdd:PRK10246 544 EEGAALR-----GQLD--ALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldAQEEHERQlrlls 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 906 ----------GLERQVAGLQQEKESLQEKLKAAKAAAG-SLPGLQAQ---LAQAEQRAQSLQeAAHQELNTLKFQLSA-- 969
Cdd:PRK10246 617 qrhelqgqiaAHNQQIIQYQQQIEQRQQQLLTALAGYAlTLPQEDEEaswLATRQQEAQSWQ-QRQNELTALQNRIQQlt 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 970 ---------EIMDYQS------RLKNAGEECKSLRGQLEEQGRQlqaaeEAVEKLKATQADMGEKLSCTSNHLAECQA-- 1032
Cdd:PRK10246 696 plletlpqsDDLPHSEetvaldNWRQVHEQCLSLHSQLQTLQQQ-----DVLEAQRLQKAQAQFDTALQASVFDDQQAfl 770
|
570 580
....*....|....*....|....*...
gi 1894925300 1033 AMLRKDKEGAALREDLERTQKELEKATT 1060
Cdd:PRK10246 771 AALLDEETLTQLEQLKQNLENQRQQAQT 798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-412 |
8.27e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 186 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVT 265
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 266 QAT-----------QNTVKELQTCLQGLELGAAEKEEDYHTALRRLESM---LQPLAQELEATRDSLDKKNQHLASFPGW 331
Cdd:TIGR02168 851 SEDieslaaeieelEELIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 332 LAMAQQKADT--------ASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVN-------RQQSAQLEQLVKELQ 396
Cdd:TIGR02168 931 LEGLEVRIDNlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaaieeyEELKERYDFLTAQKE 1010
|
250
....*....|....*.
gi 1894925300 397 LKEDARASLERLVKEM 412
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEI 1026
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
646-1127 |
1.05e-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: 50.11 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 646 KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQ----CQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptd 721
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAqrkaIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLC------- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 722 NEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQdKVQSQLSMAEA--VLREHKTLVQQLKE--QNEAL 797
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-RVQAENARLEMhfKLKEDHEKIQHLEEeyKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 798 NRAHVQELL--QCSEREGALQ------EERADEAQQREEELRALQEELSQA--KCSSEEAQLEHAELQEQLHRANTDTAE 867
Cdd:pfam05483 237 DKEKQVSLLliQITEKENKMKdltfllEESRDKANQLEEKTKLQDENLKELieKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 868 LGIQV-----CALTVEKErveealaCAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLP-GLQAQ 941
Cdd:pfam05483 317 EDLQIatktiCQLTEEKE-------AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 942 LAQAEQRAQsLQEAAHQELNTLKFQLSAE--IMDYQSRLKNAGEEcksLRGQLEEQGRQLQAAEEAVEKLKATQADMGEK 1019
Cdd:pfam05483 390 SSELEEMTK-FKNNKEVELEELKKILAEDekLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1020 LSCTSNHLAECQAAMLR---KDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKY 1096
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
490 500 510
....*....|....*....|....*....|.
gi 1894925300 1097 LEErliELLRDKDALWQKSDALEFQQKLSAE 1127
Cdd:pfam05483 546 LRD---ELESVREEFIQKGDEVKCKLDKSEE 573
|
|
| RUN_RUNDC3A |
cd17699 |
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ... |
27-122 |
1.18e-05 |
|
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: 46.94 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 27 KKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWYYARSPFLQPKl 106
Cdd:cd17699 56 QRGFWDYIRLACSKV--PNNCISSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAIMLREE- 132
|
90
....*....|....*.
gi 1894925300 107 SSDIVGQLYELTEVQF 122
Cdd:cd17699 133 STVLTGMLIGLSAIDF 148
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
737-1101 |
1.29e-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: 50.02 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 737 QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTL-------VQQLKEQNEALNRAHVQELLQCS 809
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKikelekqLNQLKSEISDLNNQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 810 EREGALQEERADEAQ----QREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEA 885
Cdd:TIGR04523 313 KSELKNQEKKLEEIQnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 886 LACAVQELQDAKEaasrEREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEAAHQ------E 959
Cdd:TIGR04523 393 INDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIER----------LKETIIKNNSEIKDLTNQDSVkeliikN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 960 LNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDK 1039
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1040 EGAALREDLER-----TQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERL 1101
Cdd:TIGR04523 539 KISDLEDELNKddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| FYVE_protrudin |
cd15723 |
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ... |
1139-1190 |
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 1894925300 1139 CLDCKREFS-WMVRRHHCRICGRIFCYYCCNNYVLSKHGG------KKE--RCCRACFQKL 1190
Cdd:cd15723 2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVPRSVMGatapaaQREtvFVCSGCNDKL 62
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
658-923 |
1.38e-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: 49.51 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 658 KEAILQSKEGECQQLREEVEQCQQLA------------------EARHRELRA----LESQCQQQTQLIEVLTAE-KGQQ 714
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAAnrqrekekerykrdreqwERQRRELESrvaeLKEELRQSREKHEELEEKyKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 715 GVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQN 794
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 795 EALNRAHVQELLQCSEREGALQE---------ERADEAQQRE-------EELRALQEELSQAKCSSEEAQLEHAEL---- 854
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQlqdtittltQKLTTAHRKEaeneallEELRSLQERLNASERKVEGLGEELSSMaaqr 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 855 ---QEQLHRANTDTAELGIQVCALTVEkerVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQE 923
Cdd:pfam07888 268 drtQAELHQARLQAAQLTLQLADASLA---LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
206-1008 |
1.61e-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: 49.79 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 206 EKQLRERMQQLDRENQElRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEvtQATQNTVKELQTCLQGLELG 285
Cdd:pfam01576 270 EAQISELQEDLESERAA-RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKRE--QEVTELKKALEEETRSHEAQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 286 AAEKEEDYHTALRRLESMLQPLA---QELEATRDSLDKKNQHLasfpgwlamaQQKADTASDTKGRQEPIPSDAAQEMQE 362
Cdd:pfam01576 347 LQEMRQKHTQALEELTEQLEQAKrnkANLEKAKQALESENAEL----------QAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 363 LGEKLQALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKEMAPLQEELsgkgQEADQLwrrLQELLAHTSS 442
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSELESVSSLL---NEAEGKNIKLSKDVSSLESQL----QDTQEL---LQEETRQKLN 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 443 WEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLA-------QVSQHVSDLEEQKKQLIQDKDHLSQQvgMLER 515
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSdmkkkleEDAGTLEALEEGKKRLQRELEALTQQ--LEEK 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 516 LAGPPGPELP---VAGEKNEALVPVNSSLQEAwGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELqnvvgRN 592
Cdd:pfam01576 565 AAAYDKLEKTknrLQQELDDLLVDLDHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKET-----RA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 593 QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGecQQL 672
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED--AKL 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 673 REEVeqcqqlaearhrELRALESQCQQQTQLIEVLTAEKGQQGVgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQV 752
Cdd:pfam01576 717 RLEV------------NMQALKAQFERDLQARDEQGEEKRRQLV-----KQVRELEAELEDERKQRAQAVAAKKKLELDL 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 753 VDLQAKMRAALDDQDKVQSQLSMAEAVLREHKtlvqqlKEQNEAlnRAHVQELLQCSeregalqEERADEAQQREEELRA 832
Cdd:pfam01576 780 KELEAQIDAANKGREEAVKQLKKLQAQMKDLQ------RELEEA--RASRDEILAQS-------KESEKKLKNLEAELLQ 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 833 LQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAelgiqvcALTVEKERVEEALACAVQELQDAKEAAsrerEGLERQVA 912
Cdd:pfam01576 845 LQEDLAASERARRQAQQERDELADEIASGASGKS-------ALQDEKRRLEARIAQLEEELEEEQSNT----ELLNDRLR 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 913 GLQQEKESLQEKLKAAKAAAGSLPGLQAQLaqaEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEeckslrgQL 992
Cdd:pfam01576 914 KSTLQVEQLTTELAAERSTSQKSESARQQL---ERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEE-------QL 983
|
810
....*....|....*.
gi 1894925300 993 EEQGRQLQAAEEAVEK 1008
Cdd:pfam01576 984 EQESRERQAANKLVRR 999
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
356-1002 |
2.07e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 356 AAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQE--------ELSGKGQEAD 427
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpqlaalSLAQPARQLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 428 QLWRRLQEllaHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEE------------- 494
Cdd:PRK10246 294 PHWERIQE---QSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRfrqwnnelagwra 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 495 QKKQLIQDKDHLSQQVGML-----ERLAGPPGPELPVAGEKNEALVPVN---------SSLQEAWGKPEEEQRGLQEA-- 558
Cdd:PRK10246 371 QFSQQTSDREQLRQWQQQLthaeqKLNALPAITLTLTADEVAAALAQHAeqrplrqrlVALHGQIVPQQKRLAQLQVAiq 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 559 QLDDTKVQEGSQEEELRQANRELEKELQNVVG------RNQLLEGKLQALQA----------------DYQALQQreSAI 616
Cdd:PRK10246 451 NVTQEQTQRNAALNEMRQRYKEKTQQLADVKTiceqeaRIKDLEAQRAQLQAgqpcplcgstshpaveAYQALEP--GVN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 617 QGSLASLEAEQASIRHLGdqmeaslLAVRKAKEAMKAQmaekeaiLQSKEGECQQLREEVeqcQQLAEARHRELRALESQ 696
Cdd:PRK10246 529 QSRLDALEKEVKKLGEEG-------AALRGQLDALTKQ-------LQRDESEAQSLRQEE---QALTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 697 CQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALsQAQLEVHQGEVQRLQAQVVDLQAKMRAALD-------DQDKV 769
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHE-------RQLRLLSQRHEL-QGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltlpQEDEE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 770 QSQLSMAEAvlrEHKTLVQQLKEQNEALNR-AHVQELLQCSEREGALQEERADEAQqreEELRALQEElsqakCSSEEAQ 848
Cdd:PRK10246 664 ASWLATRQQ---EAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVAL---DNWRQVHEQ-----CLSLHSQ 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 849 LEHAELQEQLHRANTDTAElgiqvcaltvekERVEEALACAVQELQDAKEAASREREGLERqvagLQQEKESLQEKLKAA 928
Cdd:PRK10246 733 LQTLQQQDVLEAQRLQKAQ------------AQFDTALQASVFDDQQAFLAALLDEETLTQ----LEQLKQNLENQRQQA 796
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 929 KAaagslpgLQAQLAQAEQRAQSLQEAAHQELNTLKfQLSAEIMDYQSRLKNAGEECKSLRGQL--EEQGRQLQAA 1002
Cdd:PRK10246 797 QT-------LVTQTAQALAQHQQHRPDGLDLTVTVE-QIQQELAQLAQQLRENTTRQGEIRQQLkqDADNRQQQQA 864
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
569-1125 |
2.41e-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: 48.86 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 569 SQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQ---MEASLLAVR 645
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQiseLKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 646 KAKEAMKAQMAEKEAILQSKEGECQQLREE-------VEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKgQQGVGP 718
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 719 PTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaeavlREHKTLVQQLKEQNEALN 798
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-------EEKQNEIEKLKKENQSYK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 799 RAHVQELLQCSEREGALQEERaDEAQQREEELRALQEELsqakcssEEAQLEHAELQEQLHRANTDTAELgiqvcaltve 878
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQE-KLNQQKDEQIKKLQQEK-------ELLEKEIERLKETIIKNNSEIKDL---------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 879 kERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAagsLPGLQAQLAQAEQRAQSLQE---- 954
Cdd:TIGR04523 446 -TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE---LKKLNEEKKELEEKVKDLTKkiss 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 955 --AAHQELNTLKFQLSAEIMDYQSRLKNAGEECKS--LRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEC 1030
Cdd:TIGR04523 522 lkEKIEKLESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1031 QAAMLRKDKEGAALREDLERTQKELEKATT---KIQEYYNKLCQEVTNRE---RNDQKMLADLDDLNRTKKYLEERLIEL 1104
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEVKQIKetiKEIRNKWPEIIKKIKESKTKIDDIIEL 681
|
570 580
....*....|....*....|.
gi 1894925300 1105 LRDkdalWQKSDALEFQQKLS 1125
Cdd:TIGR04523 682 MKD----WLKELSLHYKKYIT 698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
200-438 |
2.61e-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: 48.22 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 200 DQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQterergrtaaednvrltclvaELQKQWEVTQATQNTVKELQTCL 279
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---------------------QLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 280 QGLELGAAEKEEDYHTALRRLESMLQPLAQEL-EATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIpSDAAQ 358
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 359 EMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLErlvKEMAPLQEELSGKGQEADQLWRRLQELLA 438
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEA 234
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
201-765 |
2.62e-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: 48.81 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 201 QLEVREKQLRERMQQLDRENQELRAAVSQQGE-QLQTERERGRTAAEDNVRL-----TCLVAELQKQWEVTQATQNTVKE 274
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDahevaTSIREISCQQHTLTQHIHTLQQQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 275 LQTCLQGLELGAAEKEEdyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDTKGRQEPIPS 354
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDI-----LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 355 DAAQEMQELGEKLQALER-----ERTKVEEVNRQQSAQLEQLVKELQLKEDARAS-----LERLVKEMAPLQEELSGKGQ 424
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLET 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 425 EADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQH------VSDLEEQKKQ 498
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAedmlacEQHALLRKLQ 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 499 LIQDKDHLSQQVGMLER-----LAGPPGPELPVAGEKNEALVPVNSSLQEAWGkpeeEQRGLQEAQLDDTKVQEGSQEEE 573
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQelalkLTALHALQLTLTQERVREHALSIRVLPKELL----ASRQLALQKMQSEKEQLTYWKEM 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 574 LRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASirhlgdqmeasllaVRKAKEAMKA 653
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART--------------VLKARTEAHF 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 654 QMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQT---QLIEVLTAEKGQQGVgPPTDNEARELAAQ 730
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdEDILNLQCETLVQEE-EQFLSRLEEKSAT 843
|
570 580 590
....*....|....*....|....*....|....*
gi 1894925300 731 LALSQAQLEvHQGEVQRLQAQVVDLQAKMRAALDD 765
Cdd:TIGR00618 844 LGEITHQLL-KYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
550-860 |
2.86e-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: 48.58 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 550 EEQRGLQEAQlddtkvqEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGS-LASLEAEQA 628
Cdd:pfam17380 313 ERRRKLEEAE-------KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISrMRELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 629 SIRHLGDQMEASLLAVRKakeaMKAQMAEKEAILQSKEGECQQLREEVEqcqqlaEARHRELRALESQCQQQTQLIEVLT 708
Cdd:pfam17380 386 ERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMEQIRAEQE------EARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 709 AEKgQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQsqlsMAEAVLREHKTLVQ 788
Cdd:pfam17380 456 QER-QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK----LLEKEMEERQKAIY 530
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 789 QLKEQNEAlnrahvqellqcseregalQEERadEAQQREEELRALQEELSQAkcSSEEAQLEHAELQEQLHR 860
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 ... |
573-708 |
2.86e-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: 47.88 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 573 ELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQ--------------ASIRHLGDQME 638
Cdd:pfam15905 160 ELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKieekseteklleyiTELSCVSEQVE 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 639 ASLLAVRKAKEAMKAQMAE----KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLT 708
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEieslKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELK 313
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
355-690 |
3.01e-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: 48.80 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 355 DAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLkedarasLERLVKEMAPLQEE-LSGKGQEADQLWRRL 433
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-------LNKLLPQANLLADEtLADRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 434 QELLAHTSSweeelaelrrekkqqqeekelLEQEVRSLTRQLQFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQV 510
Cdd:COG3096 906 QEAQAFIQQ---------------------HGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVV 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 511 GMLERLagppgpelpvAGEKNEALVPVNSSLQEAWgkpeeeqrglqEAQLDDTKVQEGSQEEELRQANRELEKELQnvvg 590
Cdd:COG3096 965 QRRPHF----------SYEDAVGLLGENSDLNEKL-----------RARLEQAEEARREAREQLRQAQAQYSQYNQ---- 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 591 RNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHlgDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGEC- 669
Cdd:COG3096 1020 VLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRR--DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLr 1097
|
330 340 350
....*....|....*....|....*....|..
gi 1894925300 670 ------QQLREEVEQ-----CQQLAEARHREL 690
Cdd:COG3096 1098 kaerdyKQEREQVVQakagwCAVLRLARDNDV 1129
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
571-951 |
3.50e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 571 EEELRQanrELeKELQNVVGRNQLleGKLQALQADYQALQQResaiQGSLASLEAEQASI-------RHLGDQMEASLLA 643
Cdd:PRK10929 25 EKQITQ---EL-EQAKAAKTPAQA--EIVEALQSALNWLEER----KGSLERAKQYQQVIdnfpklsAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 644 VRKAKEAMKAQMAEKEaILQSKegecQQLREEVEQCQQLAEaRHRELRALESQC-QQQTQLIEVLT-AEKGQQGVGPPTD 721
Cdd:PRK10929 95 PRSVPPNMSTDALEQE-ILQVS----SQLLEKSRQAQQEQD-RAREISDSLSQLpQQQTEARRQLNeIERRLQTLGTPNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 722 nearelaaqlALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEavlREHKTLVQQLKEQNEALNRAH 801
Cdd:PRK10929 169 ----------PLAQAQLTALQAESAALKALVDELELAQLSANNRQELARLRSELAK---KRSQQLDAYLQALRNQLNSQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 802 VQELLQCSEREGALQEERADEAQQREEELRaLQEELSQAkcSSEEAQlEHAELQEQLHRANTDTaelgIQV-CALTVEKE 880
Cdd:PRK10929 236 QREAERALESTELLAEQSGDLPKSIVAQFK-INRELSQA--LNQQAQ-RMDLIASQQRQAASQT----LQVrQALNTLRE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 881 RVE---------EALACAVQELQDAKEAASREREGLERQVAGLQQEK--ESLQEKLKAAKAAAGSLPGLQAQLAQAEQRA 949
Cdd:PRK10929 308 QSQwlgvsnalgEALRAQVARLPEMPKPQQLDTEMAQLRVQRLRYEDllNKQPQLRQIRQADGQPLTAEQNRILDAQLRT 387
|
..
gi 1894925300 950 QS 951
Cdd:PRK10929 388 QR 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
472-806 |
3.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 472 TRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAG------EKNEALVPVNSS----- 540
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiaELEAELERLDASsddla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 541 -LQEAWGKPEEEQRGLQEaQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLE-GKLQALQADYQAL--QQRESAI 616
Cdd:COG4913 689 aLEEQLEELEAELEELEE-ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAAlgDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 617 QGSL-ASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEveqcqQLAEARHRELRALES 695
Cdd:COG4913 768 RENLeERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED-----GLPEYEERFKELLNE 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 696 QCQQ-QTQLIEVLTAEKgqqgvgpptdNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAkMRAALDDQDKVQSQLS 774
Cdd:COG4913 843 NSIEfVADLLSKLRRAI----------REIKERIDPLNDSLKRIPFGPGRYLRLEARPRPDPE-VREFRQELRAVTSGAS 911
|
330 340 350
....*....|....*....|....*....|....*..
gi 1894925300 775 MAEAVLREH-----KTLVQQLKEQNEALNRAHVQELL 806
Cdd:COG4913 912 LFDEELSEArfaalKRLIERLRSEEEESDRRWRARVL 948
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
600-1056 |
5.41e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 600 QALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 679
Cdd:COG3899 770 RALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREA 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 680 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKM 759
Cdd:COG3899 850 LELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAA 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 760 RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQ 839
Cdd:COG3899 930 ALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAA 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 840 AkCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKE 919
Cdd:COG3899 1010 A-AAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAAL 1088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 920 SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQL 999
Cdd:COG3899 1089 AAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAA 1168
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1000 QAAEEAVEKLKATQADMGEKLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELE 1056
Cdd:COG3899 1169 LALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
779-1119 |
6.22e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 779 VLREHKTL--VQQLKEQNEALNRAHvQELLQCSEREGALQ--EERADEAQQREEELRALQEELSQAKcsSEEAQLEHAEL 854
Cdd:COG4913 217 MLEEPDTFeaADALVEHFDDLERAH-EALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALR--LWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 855 QEQLHRantdtaelgiqvcaLTVEKERVEEALAcavqELQDAKEAASREREGLERQVAGLQ-QEKESLQEKLKaakaaag 933
Cdd:COG4913 294 EAELEE--------------LRAELARLEAELE----RLEARLDALREELDELEAQIRGNGgDRLEQLEREIE------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 934 slpGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAEImdyqsrlknagEECKSLRGQLEEQGRQLQAAEEAVEKLKAtq 1013
Cdd:COG4913 349 ---RLERELEERERRRARLEAL----LAALGLPLPASA-----------EEFAALRAEAAALLEALEEELEALEEALA-- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1014 admgeklsctsnhlaecqaamlrkdkegaalreDLERTQKELEKATTKIQeyynklcQEVTNRERN----DQKMLADLDD 1089
Cdd:COG4913 409 ---------------------------------EAEAALRDLRRELRELE-------AEIASLERRksniPARLLALRDA 448
|
330 340 350
....*....|....*....|....*....|....*
gi 1894925300 1090 LNRTKKYLEERL---IELL--RDKDALWQksDALE 1119
Cdd:COG4913 449 LAEALGLDEAELpfvGELIevRPEEERWR--GAIE 481
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
658-925 |
6.48e-05 |
|
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: 46.98 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 658 KEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVgpptdnEARELAAQLALSQAQ 737
Cdd:pfam15742 4 GEKLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKA------ELKQAQQKLLDSTKM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 738 LEVHQGEVQRLQAQVVDLQAKMraaLDDQDKVQSQLSMAEAVLREHKTLVQQLK---EQNEALNRAHVQELLQCSEREGA 814
Cdd:pfam15742 78 CSSLTAEWKHCQQKIRELELEV---LKQAQSIKSQNSLQEKLAQEKSRVADAEEkilELQQKLEHAHKVCLTDTCILEKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 815 LQEERADEAQQREEELRA-LQEELSQAKCSSEEAQlehaELQEQLhRANTDTAELGIQVCALTVEKERVEEALACAVQEL 893
Cdd:pfam15742 155 QLEERIKEASENEAKLKQqYQEEQQKRKLLDQNVN----ELQQQV-RSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENE 229
|
250 260 270
....*....|....*....|....*....|..
gi 1894925300 894 QDAKEAASREREGLERQVAGLQQEKESLQEKL 925
Cdd:pfam15742 230 KRKSDEHLKSNQELSEKLSSLQQEKEALQEEL 261
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
233-886 |
7.33e-05 |
|
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: 47.51 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 233 QLQTERERgrtAAEDNVRLTCLVAELQKQWEVTQATQNT----VKELQTCLQGLELGAAEKEED---------YHTALRR 299
Cdd:pfam10174 120 RLQSEHER---QAKELFLLRKTLEEMELRIETQKQTLGArdesIKKLLEMLQSKGLPKKSGEEDwertrriaeAEMQLGH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 300 LESMLQPLAQELEATRDSLDKKNQhlasfpgwlamaqqkadtasdtkGRQEPIPSDAAQEMQELGE-KLQALERERTKVE 378
Cdd:pfam10174 197 LEVLLDQKEKENIHLREELHRRNQ-----------------------LQPDPAKTKALQTVIEMKDtKISSLERNIRDLE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 379 -EVNRQQSAQL---EQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRREK 454
Cdd:pfam10174 254 dEVQMLKTNGLlhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 455 KQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERlagppgpELPVAGEKNEAL 534
Cdd:pfam10174 334 TAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 535 VPVNSSLQEAWGKPEEEQRGLQ--------------EAQLDDTKVQEGSQEEELRQaNRELEKELQNVVGRNQLLEGKLQ 600
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQtdssntdtalttleEALSEKERIIERLKEQRERE-DRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 601 ALQADYQA-------LQQRESAIQGS-------LASLEAEQASIRHLGDQMEASLLAVRKAKEA--MKAQMAEKeaiLQS 664
Cdd:pfam10174 486 ALQPELTEkesslidLKEHASSLASSglkkdskLKSLEIAVEQKKEECSKLENQLKKAHNAEEAvrTNPEINDR---IRL 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 665 KEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQGVGPPTdnearelaaqlalSQAQLEVHQGE 744
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNK-------------KVANIKHGQQE 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 745 VQRLQAQVVDLQakmRAALDDQDKVQSQLSMAEAVLREHKTLvQQLKEQNEALnrAHVQELLQcsEREGALQEERADEAQ 824
Cdd:pfam10174 630 MKKKGAQLLEEA---RRREDNLADNSQQLQLEELMGALEKTR-QELDATKARL--SSTQQSLA--EKDGHLTNLRAERRK 701
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 825 QREEELRALQEELsQAKCSSEEAQLEHAELQEQLHRANTDtaelgiQVCALTVEKERVEEAL 886
Cdd:pfam10174 702 QLEEILEMKQEAL-LAAISEKDANIALLELSSSKKKKTQE------EVMALKREKDRLVHQL 756
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
546-1114 |
7.98e-05 |
|
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: 47.12 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 546 GKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEG--KLQALQADYQALQQRESAIQGSLASL 623
Cdd:pfam10174 173 PKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDpaKTKALQTVIEMKDTKISSLERNIRDL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 624 EAEQASIRHLGD-----------QMEAsllaVRKAKEAMKAQMAEKEAILQSKEGE-----------------CQQ---- 671
Cdd:pfam10174 253 EDEVQMLKTNGLlhtedreeeikQMEV----YKSHSKFMKNKIDQLKQELSKKESEllalqtkletltnqnsdCKQhiev 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 672 LREEVEQCQQLAEARHRELRAL-------ESQCQQQTQLIEVLTAEKGQQGvgpptdNEARELAAQLALSQAQLEVHQGE 744
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALrlrleekESFLNKKTKQLQDLTEEKSTLA------GEIRDLKDMLDVKERKINVLQKK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 745 VQRLQAQVVD-------LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELlqcseregalqE 817
Cdd:pfam10174 403 IENLQEQLRDkdkqlagLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEEL-----------E 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 818 ERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVcaltveKERVEEALACAVQeLQDAK 897
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV------EQKKEECSKLENQ-LKKAH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 898 EAASREREGLE--RQVAGLQQEKESLQEKlkaAKAAAGSLPGLQAQLAQAEQRA----------QSLQEAAHQELNTLKF 965
Cdd:pfam10174 545 NAEEAVRTNPEinDRIRLLEQEVARYKEE---SGKAQAEVERLLGILREVENEKndkdkkiaelESLTLRQMKEQNKKVA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 966 QLSAeiMDYQSRLKNAGEECKSLRGQLEE----QGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAEcqaamlrKDKEG 1041
Cdd:pfam10174 622 NIKH--GQQEMKKKGAQLLEEARRREDNLadnsQQLQLEELMGALEKTRQELDATKARLSSTQQSLAE-------KDGHL 692
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 1042 AALRedLERtQKELEKATTKIQEyynKLCQEVTNRERNdqkmLADLDDLNRTKKYLEERLIELLRDKDALWQK 1114
Cdd:pfam10174 693 TNLR--AER-RKQLEEILEMKQE---ALLAAISEKDAN----IALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-765 |
8.65e-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: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 196 RLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERgrtaaednvrltclVAELQKQWEvtQATQNTVKEL 275
Cdd:COG4913 280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE--------------LDELEAQIR--GNGGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 276 QTCLQGLELGAAEKE---EDYHTALRRLESMLQPLAQELEATRDSLDkknQHLASFPGWLAMAQQKADTASDTKgrqepi 352
Cdd:COG4913 344 EREIERLERELEERErrrARLEALLAALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAAL------ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 353 pSDAAQEMQELGEKLQALERERTKVEEvnRQQSAqLEQLVKELQLKEDaraslerlvkEMAPLQEELSGKGQEADqlWRR 432
Cdd:COG4913 415 -RDLRRELRELEAEIASLERRKSNIPA--RLLAL-RDALAEALGLDEA----------ELPFVGELIEVRPEEER--WRG 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 433 LQELLAHTSSweeelaelrrekkqqqeekelleqevRSLtrqlqfL--ETQLAQVSQHVSDLeeqkkqliqdkdHLSQQV 510
Cdd:COG4913 479 AIERVLGGFA--------------------------LTL------LvpPEHYAAALRWVNRL------------HLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 511 gMLERLAGPPGPELPVAGEKNE--ALVPVNSSLQEAWGKPEEEQRGL-----QEAQLDDTK---VQEG--SQEEELRQAN 578
Cdd:COG4913 515 -VYERVRTGLPDPERPRLDPDSlaGKLDFKPHPFRAWLEAELGRRFDyvcvdSPEELRRHPraiTRAGqvKGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 579 RELEKELQNVVGRN-----QLLEGKLQALQADYQALQQRESAIQGSLASLEAEQASIRHLgDQMEASLLAVRKAKEAMKA 653
Cdd:COG4913 594 DRRRIRSRYVLGFDnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 654 QMAEKEAILQSKeGECQQLREEVEQCQQLAEARHRELRALESQC----QQQTQLIEVLTAEKGQQGVGPPTDNEARELAA 729
Cdd:COG4913 673 LEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
570 580 590
....*....|....*....|....*....|....*..
gi 1894925300 730 QLALSQAQLEVHQGEVQR-LQAQVVDLQAKMRAALDD 765
Cdd:COG4913 752 EERFAAALGDAVERELREnLEERIDALRARLNRAEEE 788
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
336-782 |
9.95e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 336 QQKADTASDTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLV------ 409
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 410 KEMAPLQEELSGKGQEADQLWRRLQELLAHTSSWEEELAELRRE----KKQQQEEKELLEQEVRSLTRQLQFLETQLAQV 485
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELqeelEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 486 SQHVSDLEEQKKQLIQDKDHLSQQ-------------------VGMLERLAGPPGPELPVAGEKNEALVPVNS--SLQEA 544
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENEleaaaleerlkearlllliAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 545 WGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQgsLASLE 624
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 625 AEQasirhlgdqmeASLLAvrkakeamKAQMAEKEailqskegecqQLREEVEQCQQLAEARhRELRALESQCQQQTQLI 704
Cdd:COG4717 370 QEI-----------AALLA--------EAGVEDEE-----------ELRAALEQAEEYQELK-EELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 705 EVLTAekgqqgvgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQ--DKVQSQLSMAEAVLRE 782
Cdd:COG4717 419 EELLE-----------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
816-1016 |
1.26e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 816 QEERADEAQQReeeLRALQEELSQAKcsseeAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALAcavqELQD 895
Cdd:COG3206 166 LELRREEARKA---LEFLEEQLPELR-----KELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLA----EARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 896 AKEAASREREGLERQVAGLQQEKESLQEklkaakaaAGSLPGLQAQLAQAEQRAQSLQE----------AAHQELNTLKF 965
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 966 QLSAEIMDYQSRLKNageECKSLRGQLEEQGRQLQAAEEAVEKLKATQADM 1016
Cdd:COG3206 306 QLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| RUN_RUFY1 |
cd17694 |
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ... |
11-95 |
1.45e-04 |
|
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: 43.74 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 11 ETC-KFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTK 89
Cdd:cd17694 42 EHClKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKD 121
|
....*.
gi 1894925300 90 VTSDWY 95
Cdd:cd17694 122 LLSEFY 127
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
556-838 |
1.57e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 556 QEAQLDDTKVQEGSQEEELRQANRELE--KELQNVVGRNQL-------LEGKLQALQADYQALQQRESAIQGSLASLEAe 626
Cdd:PRK11281 78 QKEETEQLKQQLAQAPAKLRQAQAELEalKDDNDEETRETLstlslrqLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 627 qASIRhlgdqmeasllaVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVeqcQQLAEArhrELRALESQCQQQTQLIEV 706
Cdd:PRK11281 157 -QPER------------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ---RVLLQA---EQALLNAQNDLQRKSLEG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 707 LTaekgqqgvgpptdnearelaaQL-ALSQAQLEVHQGEVQRLQAQVVDLQakmrAALDDQDKVQSQLSMAEAVLREHKT 785
Cdd:PRK11281 218 NT---------------------QLqDLLQKQRDYLTARIQRLEHQLQLLQ----EAINSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 786 LVQQ--LKEQNEALNRAHVQELLQCSEREGAL--QEERA----DEAQQREeelRALQEELS 838
Cdd:PRK11281 273 RIQAnpLVAQELEINLQLSQRLLKATEKLNTLtqQNLRVknwlDRLTQSE---RNIKEQIS 330
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
209-918 |
1.79e-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: 46.28 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 209 LRERMQQLDRENQELRaavsQQGEQLQTERErgrTAAEDNVRLTCLVAELQKQWEVTQATQNTVKELQTCLQGLELGAAE 288
Cdd:pfam07111 61 LSQQAELISRQLQELR----RLEEEVRLLRE---TSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 289 KEEDYHTALRRLESMLQplaqeleatrdsldkknQHLASfpgwLAMAQQKA--DTASDTKGRQEPIPSdaaQEMQELGEK 366
Cdd:pfam07111 134 LEEGSQRELEEIQRLHQ-----------------EQLSS----LTQAHEEAlsSLTSKAEGLEKSLNS---LETKRAGEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 367 LQALERERtKVEEVNRQQSAQLEQLVKELQLKEdaraSLERLVKEMAPLQEELSGKGQEADQLWRRLQELLAHTSSweee 446
Cdd:pfam07111 190 KQLAEAQK-EAELLRKQLSKTQEELEAQVTLVE----SLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRAD---- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 447 laelrrekkqQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQ-----------------------KKQLIQDK 503
Cdd:pfam07111 261 ----------LQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEfpkkcrsllnrwrekvfalmvqlKAQDLEHR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 504 DHLSQQVGMLERLAgppgpELPVAGEKNEALvpVNSSLQEAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANreLEK 583
Cdd:pfam07111 331 DSVKQLRGQVAELQ-----EQVTSQSQEQAI--LQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTAS--AEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 584 ELQNVVGrnqllegklqalqadyqALQQRESAIQGSLASLEAEQASIRHLGDQMEaslLAVRKAkEAMKAQMAEKEAILQ 663
Cdd:pfam07111 402 QLKFVVN-----------------AMSSTQIWLETTMTRVEQAVARIPSLSNRLS---YAVRKV-HTIKGLMARKVALAQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 664 SKEGEC------QQLREEVE-QCQQLAEARHRelraLESQCQQQTQLIevltaekgQQGVGpptdnEARElaaqlalsqa 736
Cdd:pfam07111 461 LRQESCpppppaPPVDADLSlELEQLREERNR----LDAELQLSAHLI--------QQEVG-----RARE---------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 737 qlevhQGEVQRLQAQVVDLQAkmraaldDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAhvQELLQCSEREGALQ 816
Cdd:pfam07111 514 -----QGEAERQQLSEVAQQL-------EQELQRAQESLASVGQQLEVARQGQQESTEEAASLR--QELTQQQEIYGQAL 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 817 EERADEAQQReeelraLQEELSQAKCSSEEAQLEHAE----LQEQLHRAntdtaelgiqvcalTVEKERVEEalacaVQE 892
Cdd:pfam07111 580 QEKVAEVETR------LREQLSDTKRRLNEARREQAKavvsLRQIQHRA--------------TQEKERNQE-----LRR 634
|
730 740
....*....|....*....|....*.
gi 1894925300 893 LQDakEAASREREGLERQVAGLQQEK 918
Cdd:pfam07111 635 LQD--EARKEEGQRLARRVQELERDK 658
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
755-925 |
1.97e-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: 45.19 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 755 LQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQcseregalqeeradeaqqrEEELRALQ 834
Cdd:pfam15905 168 LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-------------------TEKLLEYI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 835 EELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERqvaGL 914
Cdd:pfam15905 229 TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ---TL 305
|
170
....*....|.
gi 1894925300 915 QQEKESLQEKL 925
Cdd:pfam15905 306 NAELEELKEKL 316
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
600-864 |
2.19e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 600 QALQADYQALQQRESaiqgslasLEAEQASIRHLGDQMEASLlavrKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQC 679
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 680 QQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGE----VQRLQ---AQV 752
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQ-------NDLAEYNSQLVSLQTQPERAQAAlyanSQRLQqirNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 753 VDLQAKMRAALDDQ-DKVQSQLSMAEAVLRehktLVQQLKEQNEALnrahvQELLQcSEREgalqeERADEAQQREEELR 831
Cdd:PRK11281 180 KGGKVGGKALRPSQrVLLQAEQALLNAQND----LQRKSLEGNTQL-----QDLLQ-KQRD-----YLTARIQRLEHQLQ 244
|
250 260 270
....*....|....*....|....*....|...
gi 1894925300 832 ALQEELSQAKCSSEEAQLEHAELQEQLHRANTD 864
Cdd:PRK11281 245 LLQEAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
827-1078 |
2.87e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 827 EEELRALQEELSQAKCSSEEAQLEHAELQEQLhrantdtaelgiqvcALTVEKERVEEALACAVQELQDAKEAASREREG 906
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTL---------------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 907 LERQVAGLQQEKESLQEKLkaakaaagSLPGLQAQLAQAEQRAQSLQEAahqeLNTLKFQLSAeimdYQSRLKNAGEECK 986
Cdd:PRK11281 103 LEALKDDNDEETRETLSTL--------SLRQLESRLAQTLDQLQNAQND----LAEYNSQLVS----LQTQPERAQAALY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 987 SLRGQLEEQGRQLQAAEEAVEKLKATQADMGEklscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYY 1066
Cdd:PRK11281 167 ANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ----AEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242
|
250
....*....|..
gi 1894925300 1067 NKLCQEVTNRER 1078
Cdd:PRK11281 243 LQLLQEAINSKR 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
210-411 |
3.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 210 RERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEdnvRLTCLVAELQKQWEV--TQATQNTVKELQTCLQGLELGAA 287
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE---RREALQRLAEYSWDEidVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 288 EkeedyhtaLRRLESMLQPLAQELEATRDSLDKKNQHLASFPGWLAMAQQKADTASDtkgRQEPIPSDAAQEMQELGEKL 367
Cdd:COG4913 686 D--------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEER 754
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1894925300 368 QALERERTKVEEVNRQQSAQLEQLVKELqlkEDARASLERLVKE 411
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARL---NRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
902-1085 |
3.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 902 REREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEA-AHQELNTLKFQLSAEIMDYQSRLKN 980
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 981 AGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKlscTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATT 1060
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|....*
gi 1894925300 1061 KIQEYYNKLCQEVTNRERNDQKMLA 1085
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLL 252
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
725-965 |
3.35e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 725 RELAAQLalsqaqLEVH-QGEVQRLqaqvvdLQAKM-RAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQnealnrahv 802
Cdd:COG0497 119 RELGELL------VDIHgQHEHQSL------LDPDAqRELLDAFAGLEELLEEYREAYRAWRALKKELEEL--------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 803 qellqcseregalqEERADEAQQREEELRALQEELSQAKCSS-EEAQLE-------HAE-LQEQLHRA------NTDTAE 867
Cdd:COG0497 178 --------------RADEAERARELDLLRFQLEELEAAALQPgEEEELEeerrrlsNAEkLREALQEAlealsgGEGGAL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 868 LGIQVCALTVEK------------ERVEEALAcavqELQDAKEAASREREGLE------------------------RQV 911
Cdd:COG0497 244 DLLGQALRALERlaeydpslaelaERLESALI----ELEEAASELRRYLDSLEfdperleeveerlallrrlarkygVTV 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925300 912 AGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQR---------------AQSLQEAAHQELNTLKF 965
Cdd:COG0497 320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAElleaaeklsaarkkaAKKLEKAVTAELADLGM 388
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
553-774 |
3.73e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 553 RGLQEaQLDDTKVQEGSQEEELRQANReLEKELQNVVGRNqllegkLQALQADYQALQQRESAIQGSLASLEAEQASIRH 632
Cdd:PHA02562 177 RELNQ-QIQTLDMKIDHIQQQIKTYNK-NIEEQRKKNGEN------IARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 633 LGDQMEASLLAVRKAKEAMKAQMA--EKEAILQSKEGEC----QQLREEVEQC----QQLAEARHRELRALESQCQQQTQ 702
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCptctQQISEGPDRItkikDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1894925300 703 LIEVLTAEKGQQGVgpptDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 774
Cdd:PHA02562 329 MDEFNEQSKKLLEL----KNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| FYVE_RUFY3 |
cd15744 |
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ... |
1139-1187 |
4.01e-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: 4.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1894925300 1139 CLDCKREFSWMVR-RHHCRICGRIFCYYCCNNYV-LSKHGGKKERCCRACF 1187
Cdd:cd15744 2 CSLCQEDFASLALpKHNCYNCGGTFCDACSSNELpLPSSIYEPARVCDVCY 52
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
749-911 |
4.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 749 QAQVVDLQAkmraaLDDQ-DKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERA----DEA 823
Cdd:COG1579 6 LRALLDLQE-----LDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 824 QQRE----EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDAKEA 899
Cdd:COG1579 81 QLGNvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|..
gi 1894925300 900 ASREREGLERQV 911
Cdd:COG1579 161 LEAEREELAAKI 172
|
|
| RUN_RUFY2 |
cd17695 |
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ... |
11-124 |
4.64e-04 |
|
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: 42.27 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 11 ETC-KFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTK 89
Cdd:cd17695 42 EHClKHGLKVRKSFLSYNKTIWGPLELVEKLCPEAEEIAASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRD 121
|
90 100 110
....*....|....*....|....*....|....*
gi 1894925300 90 VTSDWYYARSPFLQPKlSSDIVGQLYELTEVQFDL 124
Cdd:cd17695 122 LLSEFYEYHALMMEEE-GAVIVGLLVGLNVIDANL 155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
893-1091 |
5.13e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 893 LQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAG--SLPG------------------LQAQLAQAEQRAQSL 952
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEeaklllqqlselesqlaeARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 953 QEAAHQELNTLKFQL-SAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKLsctsnhLAECQ 1031
Cdd:COG3206 246 RAQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI------LASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1032 AAMLRKDKEGAALREDLERTQKELEKATTKIQEyYNKLCQEVTNRERNDQKMLADLDDLN 1091
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
609-1136 |
5.72e-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: 44.43 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 609 LQQRESAIQGSLASLEAEQASIRHLGDQMEASLLAVRKAKE--AMKAQMAEK-------EAILQSKEGECQQLREEV--- 676
Cdd:pfam10174 139 LEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEdwERTRRIAEAemqlghlEVLLDQKEKENIHLREELhrr 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 677 ----------EQCQQLAEARHRELRALESQCQQQTQLIEVLTAEkgqqGVGPPTDNEARELAAQLALSQA-----QLEVH 741
Cdd:pfam10174 219 nqlqpdpaktKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTN----GLLHTEDREEEIKQMEVYKSHSkfmknKIDQL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 742 QGEVQRLQAQVVDLQAKmraaLDDQDKVQSQLSMAEAVLREHKTlvqqLKEQNEALNRAHVQELLQCSEREGALQEERAD 821
Cdd:pfam10174 295 KQELSKKESELLALQTK----LETLTNQNSDCKQHIEVLKESLT----AKEQRAAILQTEVDALRLRLEEKESFLNKKTK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 822 EAQQREEELRALQEELS----------------QAKCSSEEAQLEH-----AELQE-----QLHRANTDTAeLGIQVCAL 875
Cdd:pfam10174 367 QLQDLTEEKSTLAGEIRdlkdmldvkerkinvlQKKIENLQEQLRDkdkqlAGLKErvkslQTDSSNTDTA-LTTLEEAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 876 TvEKERVEEALacavqelqdaKEAASREREGLERQVAGLQQEKESLQEKLKAakaaagslpgLQAQLAQAEQRAQSLQEA 955
Cdd:pfam10174 446 S-EKERIIERL----------KEQREREDRERLEELESLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEH 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 956 AhQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQL---EEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQA 1032
Cdd:pfam10174 505 A-SSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVER 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1033 AM--LR--------KDKEGAALREDLERTQKELEKATTKIqeyynKLCQEVTNRERNDQKMLADLDDLNRTKKYLEERLI 1102
Cdd:pfam10174 584 LLgiLRevenekndKDKKIAELESLTLRQMKEQNKKVANI-----KHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLE 658
|
570 580 590
....*....|....*....|....*....|....
gi 1894925300 1103 ELLRDKDALWQKSDALefQQKLSAEERWLGDTEA 1136
Cdd:pfam10174 659 ELMGALEKTRQELDAT--KARLSSTQQSLAEKDG 690
|
|
| FYVE_FGD3 |
cd15740 |
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ... |
1133-1187 |
6.11e-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: 6.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 1133 DTEANHCLDCKREFSWMV-RRHHCRICGRIFCYYCCNnyvLSKHGGKKERCCRACF 1187
Cdd:cd15740 2 EKEKQTCKGCNESFNSITkRRHHCKQCGAVICGKCSE---FKDLASRHNRVCRDCF 54
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
186-893 |
6.39e-04 |
|
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: 44.56 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 186 NEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQelraaVSQQGEQLQTERERGRTAAEDnvrltclVAELQKQWEVT 265
Cdd:COG3096 498 RELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQN-----AERLLEEFCQRIGQQLDAAEE-------LEELLAELEAQ 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 266 QATqntvkelqtclqgLELGAAEKEEDyHTALRRLESMLQPLAQELEATRdsldkknqhlasfPGWLAmAQQKADTASDT 345
Cdd:COG3096 566 LEE-------------LEEQAAEAVEQ-RSELRQQLEQLRARIKELAARA-------------PAWLA-AQDALERLREQ 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 346 KGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKE--------LQLKEDARASL-----ERLVKEM 412
Cdd:COG3096 618 SGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaedprlLALAERLGGVLlseiyDDVTLED 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 413 APLQEELSGKGQEA---DQLWRRLQELLAHTSS----WEEELAELRREKKQQQEEKELLEQEVRSLTRQLQ---FLETQL 482
Cdd:COG3096 698 APYFSALYGPARHAivvPDLSAVKEQLAGLEDCpedlYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRysrFPEVPL 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 483 ---AQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAgppgpelpvagEKNEALVPVNSSLQEAwGKPEEEQRGLQE-- 557
Cdd:COG3096 778 fgrAAREKRLEELRAERDELAEQYAKASFDVQKLQRLH-----------QAFSQFVGGHLAVAFA-PDPEAELAALRQrr 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 558 AQLDDTKVQEGSQEEELRQANRELEKELQNVvgrNQLLEgklQALQADYQALQQRESAIQGSLASLEAEQASIRHLGDQM 637
Cdd:COG3096 846 SELERELAQHRAQEQQLRQQLDQLKEQLQLL---NKLLP---QANLLADETLADRLEELREELDAAQEAQAFIQQHGKAL 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 638 EasllavrkakeamkaQMAEKEAILQSKEGECQQLREEVEQCQQlaearhrELRALESQCQQQTQLIEVLTAEKGQQGVG 717
Cdd:COG3096 920 A---------------QLEPLVAVLQSDPEQFEQLQADYLQAKE-------QQRRLKQQIFALSEVVQRRPHFSYEDAVG 977
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 718 ppTDNEARELAAQLalsQAQLEvhQGEVQRLQAQVvdlqaKMRAAlddqdkvQSQLSMAEAVLRE----HKTLVQQLKEQ 793
Cdd:COG3096 978 --LLGENSDLNEKL---RARLE--QAEEARREARE-----QLRQA-------QAQYSQYNQVLASlkssRDAKQQTLQEL 1038
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 794 NealnrahvQELLQCSEREGALQEERA-DEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDtaelgiqv 872
Cdd:COG3096 1039 E--------QELEELGVQADAEAEERArIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD-------- 1102
|
730 740
....*....|....*....|...
gi 1894925300 873 caLTVEKERVEEALA--CAVQEL 893
Cdd:COG3096 1103 --YKQEREQVVQAKAgwCAVLRL 1123
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
789-1129 |
6.57e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 789 QLKEQNEALNrahvqELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQlhrantdtAEL 868
Cdd:pfam17380 263 QTMTENEFLN-----QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ--------AEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 869 GIQVcALTVEKERVeealacavqelqdakeAASREREgLER-QVAGLQQEKESL-QEKLKAAKAAAGSLPGLQAQLAQAE 946
Cdd:pfam17380 330 DRQA-AIYAEQERM----------------AMERERE-LERiRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 947 QRAQSLQEAAHqelntlKFQLSAEimDYQSRLKNAGEECKSLRGQLEE-QGRQLQAAEEA----VEKLKATQADMGEKLS 1021
Cdd:pfam17380 392 ERVRQELEAAR------KVKILEE--ERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEErareMERVRLEEQERQQQVE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1022 CTSNHLAECQAAMLRKDKEgaalredlERTQKELEKATTKIQEYYNKLCQEVTNRERNDQKMLADLDDLNRTKKYLEE-- 1099
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKE--------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEErr 535
|
330 340 350
....*....|....*....|....*....|
gi 1894925300 1100 RLIELLRDKDALWQKSDALEFQQKLSAEER 1129
Cdd:pfam17380 536 REAEEERRKQQEMEERRRIQEQMRKATEER 565
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
726-896 |
6.83e-04 |
|
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: 43.51 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 726 ELAAQLALSQAQLEVhQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLK--------EQNEAL 797
Cdd:cd22656 98 ELIDDLADATDDEEL-EEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEkalkdlltDEGGAI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 798 NRAHVQELLQcseregALQEERADEAQQREEELRALQEELsqakcSSEEAQLEHAE-LQEQLHRANTDTAELgiqvcalt 876
Cdd:cd22656 177 ARKEIKDLQK------ELEKLNEEYAAKLKAKIDELKALI-----ADDEAKLAAALrLIADLTAADTDLDNL-------- 237
|
170 180
....*....|....*....|
gi 1894925300 877 veKERVEEALAcAVQELQDA 896
Cdd:cd22656 238 --LALIGPAIP-ALEKLQGA 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
939-1072 |
7.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 939 QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGE-ECKSLRGQLEEQGRQLQAAEEAVEKLKatqadmg 1017
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRLLQKEENLDRKL------- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 1018 EKLSctsnhlaecqaamlRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQE 1072
Cdd:PRK12704 103 ELLE--------------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
730-956 |
8.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 730 QLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrEHKTLVQQLKEQNEALNRAhvQELLqcs 809
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEER--REEL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 810 eregalqEERADEAQQREEELRALQEELSQakcSSEEAQLEHAELQEQLHRANTDTAElgiQVCALTVEKERVEEALACA 889
Cdd:COG3883 89 -------GERARALYRSGGSVSYLDVLLGS---ESFSDFLDRLSALSKIADADADLLE---ELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 890 VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAA 956
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
548-705 |
8.29e-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: 42.60 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 548 PEEEQRGLQEAQLDDTKVQEgsqeeeLRQANRELEKELQNvvgrnqlLEGKLQALQADYQALQQRESAIQGSLASLEAEQ 627
Cdd:COG1579 2 MPEDLRALLDLQELDSELDR------LEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 628 ASIRHLGDQMEASLLAVRKAKE---------AMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQ 698
Cdd:COG1579 69 EEVEARIKKYEEQLGNVRNNKEyealqkeieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
....*..
gi 1894925300 699 QQTQLIE 705
Cdd:COG1579 149 EELAELE 155
|
|
| GOLD_2 |
pfam13897 |
Golgi-dynamics membrane-trafficking; Sec14-like Golgi-trafficking domain The GOLD domain is ... |
1379-1424 |
8.32e-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: 8.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1894925300 1379 LIPTTRCNSHKENIQGQLKVRTPGIYMLIFDNTFSRFVSKKVFYHL 1424
Cdd:pfam13897 85 IVPVYRRDCHEEVYAGSHQYPGRGVYLLKFDNSYSLWRSKTLYYRV 130
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
548-970 |
8.83e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 548 PEEEQRGLQEAQLDDTKVQEGSQEEELRQAN-----RELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLAS 622
Cdd:COG5278 103 PEQQARLDELEALIDQWLAELEQVIALRRAGgleaaLALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 623 LEAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQ 702
Cdd:COG5278 183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 703 LIEVLTAEKGQQGVGPPTDNEARELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLRE 782
Cdd:COG5278 263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 783 HKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRAN 862
Cdd:COG5278 343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 863 TDTAELGIQVCALTVEKERVEEALACAVQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQL 942
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*...
gi 1894925300 943 AQAEQRAQSLQEAAHQELNTLKFQLSAE 970
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAEL 530
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
470-630 |
9.46e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 470 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMlerlagppgpelpvaGEKNEALVPVNSSLQEAwgkpe 549
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---------------GPDALPELLQSPVIQQL----- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 550 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVvgrNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 629
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
.
gi 1894925300 630 I 630
Cdd:COG3206 346 L 346
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
660-1009 |
9.95e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 660 AILQSKEGECQQLREEVE------QCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQ---GVGPPTDNEARELAAQ 730
Cdd:PRK10246 160 AFLNAKPKERAELLEELTgteiygQISAMVFEQHKSARTELEKLQAQASGVALLTPEQVQSltaSLQVLTDEEKQLLTAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 731 LALSQA-QLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAE--AVLR-------EHKTLVQQLKEQNEALN-R 799
Cdd:PRK10246 240 QQQQQSlNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRphweriqEQSAALAHTRQQIEEVNtR 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 800 AHVQELLQCSEREGALQEERADEAQQRE--------EELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL-GI 870
Cdd:PRK10246 320 LQSTMALRARIRHHAAKQSAELQAQQQSlntwlaehDRFRQWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLnAL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 871 QVCALTVEKERVEEALAcavqelQDAKEAASRER-EGLERQVAGLQQEKESLQEKLKAAKAAAGSLPGLQAQLAQ----- 944
Cdd:PRK10246 400 PAITLTLTADEVAAALA------QHAEQRPLRQRlVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQrykek 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 945 ----AEQRAQSLQEAAHQELNTLKFQLSA---------------------EIMDYQSRL-------KNAGEECKSLRGQL 992
Cdd:PRK10246 474 tqqlADVKTICEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLdalekevKKLGEEGAALRGQL 553
|
410
....*....|....*..
gi 1894925300 993 EEQGRQLQAAEEAVEKL 1009
Cdd:PRK10246 554 DALTKQLQRDESEAQSL 570
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
661-868 |
1.14e-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: 42.82 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 661 ILQSKEGECQQLRE---------------EVEQCQQLAEARHRELRALESQCQQ-QTQLIEVltaEKGQQgvgpptdNEA 724
Cdd:pfam09787 19 ILQSKEKLIASLKEgsgvegldsstaltlELEELRQERDLLREEIQKLRGQIQQlRTELQEL---EAQQQ-------EEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 725 RELAAQLALSQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLsmaEAVLREHKTLVQQLKEQ--NEALNRAHV 802
Cdd:pfam09787 89 ESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQltSKSQSSSSQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 803 QELlqcseregalqeeradeaqqrEEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAEL 868
Cdd:pfam09787 166 SEL---------------------ENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKEL 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-423 |
1.35e-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: 42.83 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 193 DEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDNVRLTCLVAELQKQWEVTQAT-QNT 271
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 272 VKELQTCLQGLELGAAEKEEDYHTALRRLESM------LQPLAQELEATRDSLDKKNQHLasfpgwlamAQQKADTASdt 345
Cdd:COG4942 110 LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkylapaRREQAEELRADLAELAALRAEL---------EAERAELEA-- 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1894925300 346 kgrqepipsdAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDA-RASLERLVKEMAPLQEELSGKG 423
Cdd:COG4942 179 ----------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALIARLEAEAAAAAERTPAAG 247
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
759-1078 |
1.50e-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: 43.24 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 759 MRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREgALQEERADEAQQREEELRALQEELS 838
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAE-EMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 839 QAKCSSEEAQLEHAELQEQL-----HRANTDTAELGIQVCALTVE---KERVEEALAcavqeLQDAKEAASREREGLERQ 910
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIqdleeQLDEEEAARQKLQLEKVTTEakiKKLEEDILL-----LEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 911 VAGLQQEKESLQEKLKAAKAAAGSLpglQAQLAQAEQRAQSlQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRG 990
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKH---EAMISDLEERLKK-EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 991 QLEEQGRQLQAAEEAVEKLKATQADMGEKLSCTSNHLAECQ-------AAMLRKDKEGAALREDLERTQKELEK---ATT 1060
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEALKTELEDtldTTA 316
|
330
....*....|....*...
gi 1894925300 1061 KIQEYYNKLCQEVTNRER 1078
Cdd:pfam01576 317 AQQELRSKREQEVTELKK 334
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
698-998 |
1.54e-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: 43.19 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 698 QQQTQLIEVLTAEKGQQgvgpPTDNEARELAAQLALSQAQlEVHQGEVQRlQAQVVDLQAKM---------RAALDDQDK 768
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQ----EKEEKAREVERRRKLEEAE-KARQAEMDR-QAAIYAEQERMamerereleRIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 769 V-----QSQLSMAEAVLREHKTLVQQLKEQNE----ALNRAHVQELLQcSEREGALQEE-------RADEAQQREEELRA 832
Cdd:pfam17380 361 ElerirQEEIAMEISRMRELERLQMERQQKNErvrqELEAARKVKILE-EERQRKIQQQkvemeqiRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 833 LQEELSQakcSSEEAQLEHAELQEQLHRANTDTAELGIQvcALTVEKERVEEALACAVQELQDAKEAASREREGLErqva 912
Cdd:pfam17380 440 LEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRK--KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE---- 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 913 glQQEKESLQEKlkaakaaagSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIM---DYQSRLKNAGEECKSLR 989
Cdd:pfam17380 511 --EERKRKLLEK---------EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkatEERSRLEAMEREREMMR 579
|
....*....
gi 1894925300 990 GQLEEQGRQ 998
Cdd:pfam17380 580 QIVESEKAR 588
|
|
| RUN_RUNDC3B |
cd17700 |
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ... |
18-95 |
1.59e-03 |
|
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: 40.72 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 18 KEKATLLG--NKKDYWDYFCACLAKVkgANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTKVTSDWY 95
Cdd:cd17700 45 KGQVTWFGyeSPRSFWDYIRVACSKV--PHNCICSIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFY 122
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-712 |
1.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 187 EALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRA-AVSQQGEQLQTERERGRTAA--EDNVRLTCLVAELQKQWE 263
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKleEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 264 VTQATQNTVKELQ-TCLQGLELGaaEKEEDYHTALRRLESMLQPLAQELEATRDSLDKknqhlasfpgwlamAQQKADTA 342
Cdd:PRK03918 277 ELEEKVKELKELKeKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIKE--------------LEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 343 SDTKGRQEPIpsdaAQEMQELGEKLQALERERTKVEEVNRQQSA----QLEQLVKELQLKEDARASLERLVKEmapLQEE 418
Cdd:PRK03918 341 EELKKKLKEL----EKRLEELEERHELYEEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISK---ITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 419 LSGKGQEADQLWRRLQELlahtssweeELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQHVSDLEEQKKQ 498
Cdd:PRK03918 414 IGELKKEIKELKKAIEEL---------KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 499 ----------LIQDKDHLSQQVGMLERLAGPPGPELPVAGEKNEalvpvnsSLQEAWGKPEEEQRGLQEaqlDDTKVQE- 567
Cdd:PRK03918 485 lekvlkkeseLIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-------KLKEKLIKLKGEIKSLKK---ELEKLEEl 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 568 GSQEEELRQANRELEKELQNVVGR--------NQLLEGKLQALQADYQ---ALQQRESAIQGSLASLEAEQASIrhlgDQ 636
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEEL----DK 630
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 637 MEASLLAVRKAKEAMKAQMAEKEAILQSKEGEcqQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKG 712
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
919-1129 |
1.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 919 ESLQEKLKAAKAAAGSLPGL---QAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRgqleeq 995
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE------ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 996 grQLQAAEEAVEKLKATQADMgeklsctsNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVtn 1075
Cdd:COG4717 123 --KLLQLLPLYQELEALEAEL--------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT-- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1894925300 1076 rERNDQKMLADLDDLNRTKKYLEERLIELLRDKDALWQKSDALEFQQKLSAEER 1129
Cdd:COG4717 191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
879-1020 |
1.74e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 879 KERVEEALACAVQELQDAKEAASREREGLERQVAGLQQE---KESLQEKLKaakaaaGSLPGLQAQLAQAEQRAQSLQea 955
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASlsaAEAERSRLQ------ALLAELAGAGAAAEGRAGELA-- 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1894925300 956 ahQELNTLKfQLSAEIMdyqSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLKATQADMGEKL 1020
Cdd:PRK09039 123 --QELDSEK-QVSARAL---AQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
187-893 |
2.20e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 187 EALEGFDEMRLELDQLEVREKQLRE---RMQQLDRENQELRAAVSQQGEQLQTERErgrtaaednvrltclVAELQKQWE 263
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSEleqRLRQQQRAERLLAEFCKRLGKNLDDEDE---------------LEQLQEELE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 264 VTqatqntvkelqtcLQGLELGAAEKEEDYhTALRRLESMLQPLAQELEATRdsldkknqhlasfPGWLAmAQQKADTAS 343
Cdd:PRK04863 565 AR-------------LESLSESVSEARERR-MALRQQLEQLQARIQRLAARA-------------PAWLA-AQDALARLR 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 344 DTKGRQEPIPSDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKE--------LQLKEDARASL-----ERLVK 410
Cdd:PRK04863 617 EQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPggsedprlNALAERFGGVLlseiyDDVSL 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 411 EMAPLQEELSGKGQEA------DQLWRRLQELlahtssweeelaelrrekkqqqeekelleqevRSLTRQLQFLETQLAQ 484
Cdd:PRK04863 697 EDAPYFSALYGPARHAivvpdlSDAAEQLAGL--------------------------------EDCPEDLYLIEGDPDS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 485 VSQHVSDLEEQKKQLIQDkdhLSQQVGMLERLagppgPELPVAGEKN-----EALVPVNSSLQEAWGKPEEEQRGLQEAq 559
Cdd:PRK04863 745 FDDSVFSVEELEKAVVVK---IADRQWRYSRF-----PEVPLFGRAArekriEQLRAEREELAERYATLSFDVQKLQRL- 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 560 lddtkVQEGSQ--------------EEELRQANR---ELEKELQNVVGRNQLLEGKLQALQADYQALQQRESaiQGSLAS 622
Cdd:PRK04863 816 -----HQAFSRfigshlavafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGLSALNRLLP--RLNLLA 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 623 LEAEQASIRHLGDQMEASLLAVR--KAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALesqcqqq 700
Cdd:PRK04863 889 DETLADRVEEIREQLDEAEEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL------- 961
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 701 TQLIEVLTAEKGQQGVGPPTDNEarELAAQLalsQAQLEvhQGEVQRLQAQVVDLQAKmrAALDDQDKVQSQLSMAEAVL 780
Cdd:PRK04863 962 TEVVQRRAHFSYEDAAEMLAKNS--DLNEKL---RQRLE--QAEQERTRAREQLRQAQ--AQLAQYNQVLASLKSSYDAK 1032
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 781 REhktLVQQLKEQNEALNRAHVQELlqcseregalqEERAdeAQQREEelraLQEELS--QAKCSSEEAQL-----EHAE 853
Cdd:PRK04863 1033 RQ---MLQELKQELQDLGVPADSGA-----------EERA--RARRDE----LHARLSanRSRRNQLEKQLtfceaEMDN 1092
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1894925300 854 LQEQLHRANTDtaelgiqvcaLTVEKERVEEALA--CAVQEL 893
Cdd:PRK04863 1093 LTKKLRKLERD----------YHEMREQVVNAKAgwCAVLRL 1124
|
|
| RUN_RUFY3 |
cd17696 |
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ... |
11-103 |
2.37e-03 |
|
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: 40.36 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 11 ETC-KFDQKEKATLLGNKKDYWDYFCACLAKVKGANDGIRFVKSISELRTSLGKGRAFIRYSLVHQRLADTLQQCFMNTK 89
Cdd:cd17696 42 EHClKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKD 121
|
90
....*....|....
gi 1894925300 90 VTSDWYYARSPFLQ 103
Cdd:cd17696 122 LLSEFYEPNALMME 135
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
890-1064 |
2.41e-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: 41.06 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 890 VQELQDAKEAASREREGLERQVAGLQQEKEslqeklkaakaaagslpGLQAQLAQAEQRAQSLqEAAHQELNTLKFQLSA 969
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELA-----------------ALEARLEAAKTELEDL-EKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 970 EIMDYQSRLKNAG--EECKSLRGQLEEQGRQLQAAE-------EAVEKLKATQADMGEKLSCTSNHLAECQAamlRKDKE 1040
Cdd:COG1579 74 RIKKYEEQLGNVRnnKEYEALQKEIESLKRRISDLEdeilelmERIEELEEELAELEAELAELEAELEEKKA---ELDEE 150
|
170 180
....*....|....*....|....
gi 1894925300 1041 GAALREDLERTQKELEKATTKIQE 1064
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPP 174
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
476-799 |
2.50e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 476 QFLET---QLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGMLERLAGPPGPELPVAGEK--------------------NE 532
Cdd:PRK11281 63 QDLEQtlaLLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTlslrqlesrlaqtldqlqnaQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 533 ALVPVNSSLQEAWGKPEEEQRGLQEAQ---------LDDTKVQEGSQEEELRQanrELEKELQNVVGRN----QLLEG-- 597
Cdd:PRK11281 143 DLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnlLKGGKVGGKALRPSQRV---LLQAEQALLNAQNdlqrKSLEGnt 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 598 KLQAL---QADYQALQQresaiqgslASLEAEQASIRHLGDQ--MEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQL 672
Cdd:PRK11281 220 QLQDLlqkQRDYLTARI---------QRLEHQLQLLQEAINSkrLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 673 REE-VEQCQQLAEARHRELRA---LESQCQQQTQLIEVLTAEKG---------QQGVGPPTDNEARELAAQLA-LSQAQL 738
Cdd:PRK11281 291 SQRlLKATEKLNTLTQQNLRVknwLDRLTQSERNIKEQISVLKGslllsrilyQQQQALPSADLIEGLADRIAdLRLEQF 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 739 EVHQ--GEVQRLQAQVVDLQAKMRAALDDQdkvqsqlsmaeavlrEHKTLVQQLKEQNEALNR 799
Cdd:PRK11281 371 EINQqrDALFQPDAYIDKLEAGHKSEVTDE---------------VRDALLQLLDERRELLDQ 418
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
470-705 |
2.74e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 470 SLTRQLQFLETQLAQVSQHVSDLEEQKKQLIQDKD--HLSQQVGMLErlagppgpelpvageknEALVPVNSSLQEAwgk 547
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLL-----------------QQLSELESQLAEA--- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 548 peEEQRGLQEAQLDDTKVQEGSQEEELRQANREleKELQNVVGRNQLLEGKLQALQADYQ----ALQQRESAIQGSLASL 623
Cdd:COG3206 232 --RAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 624 EAEQASIRHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAE---ARHRELRALESQCQQQ 700
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYEsllQRLEEARLAEALTVGN 387
|
....*
gi 1894925300 701 TQLIE 705
Cdd:COG3206 388 VRVID 392
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
757-894 |
2.87e-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: 40.24 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 757 AKMRAALDDQDKVQSQLS--------MAEAVLREHKTLVQQL-KEQNEAlnRAHVQEL---LQCSEREGALQEERADEAQ 824
Cdd:pfam05335 23 AQAAAAEAAARQVKNQLAdkalqaakAAEAALAGKQQIVEQLeQELREA--EAVVQEEsasLQQSQANANAAQRAAQQAQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 825 QREEELRAL----QEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELGIQVCALTVEKERVEEAL---ACAVQELQ 894
Cdd:pfam05335 101 QQLEALTAAlkaaQANLENAEQVAAGAQQELAEKTQLLEAAKKRVERLQRQLAEARADLEKTKKAAykaACAAVEAK 177
|
|
| FYVE_CARP |
cd15750 |
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ... |
1138-1186 |
3.03e-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: 36.95 E-value: 3.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1894925300 1138 HCLDCKREFSWMVRRHHCRICGRIFCYYCcnnyvLSKHGGKKeRCCRAC 1186
Cdd:cd15750 2 PCESCGAKFSVFKRKRTCADCKRYFCSNC-----LSKEERGR-RRCRRC 44
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
938-1124 |
3.06e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 938 LQAQLAQAEQRAQ--SLQEAAHQELNTLKFQLsAEIMDYQSRLKnageeckSLRGQLEEQGRQLQAAEEAVEKLKATQAD 1015
Cdd:PRK11281 41 VQAQLDALNKQKLleAEDKLVQQDLEQTLALL-DKIDRQKEETE-------QLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1016 MGE-------------KLSCTSNHLAECQAAMLRKDKEGAALREDLERTQKELEKATTKIQEYYNKLCQEVTNRE--RND 1080
Cdd:PRK11281 113 ETRetlstlslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKalRPS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1894925300 1081 QKM-----LADLD---DLNRTKKYLEERLIELLRDK-DALWQKSDALEFQQKL 1124
Cdd:PRK11281 193 QRVllqaeQALLNaqnDLQRKSLEGNTQLQDLLQKQrDYLTARIQRLEHQLQL 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
787-1129 |
3.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 787 VQQLKEQNEALNRAHVQELLQCSEREGALQEERADEAQQREEELRALQEElsqaKCSSEEAQLEHAELQEQLHRANTDTA 866
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE----RNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 867 ELGIQVCAL--TVEKERVEEAL-ACAVQELQDAKEAA--SREREGLERQVAGLQQEKESLQEKLKAAKAAAgslpglQAQ 941
Cdd:PTZ00121 1275 EEARKADELkkAEEKKKADEAKkAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAA 1348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 942 LAQAEQRAQSLQEAAHQ----ELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKL-----KAT 1012
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKaeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAE 1428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 1013 QADMGEKLSCTSNHLAecQAAMLRKDKEGAALREDLERTQKELEKA-TTKIQEYYNKLCQEVTNRERNDQKMLADLDDLN 1091
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAK--KADEAKKKAEEAKKAEEAKKKAEEAKKAdEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
330 340 350
....*....|....*....|....*....|....*....
gi 1894925300 1092 RTKKYLEE-RLIELLRDKDALWQKSDALEFQQKLSAEER 1129
Cdd:PTZ00121 1507 EAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
550-1010 |
3.82e-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: 41.65 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 550 EEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGSLASLEAEQAS 629
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 630 IRHLGD--QMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEV- 706
Cdd:pfam05557 172 IKELEFeiQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLe 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 707 LTAEKGQQ------------GVGPPTDNEARELAAQLalsQAQLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLS 774
Cdd:pfam05557 252 LEKEKLEQelqswvklaqdtGLNLRSPEDLSRRIEQL---QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 775 MAEAVLREHKTLVQQLKEQNEALN--RAHVQELLQCSEREGALQEERADEAQQREEELRALQEelSQAKCSSEEAQLEHA 852
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQRRVLLLTkeRDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQK--MQAHNEEMEAQLSVA 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 853 ELQEQLHRANTDTAELGIQVCAltvEKERVEEALACA--VQELQDAKEAASREREGLERQVAGLQQEKESLQEKLKAAKA 930
Cdd:pfam05557 407 EEELGGYKQQAQTLERELQALR---QQESLADPSYSKeeVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 931 AAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDYQSRLKNAGEECKSLRGQLEEQGRQLQAAEEAVEKLK 1010
Cdd:pfam05557 484 KTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLK 563
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
756-1021 |
4.51e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 756 QAKMRAALDDQDKVQSQLsmaeAVLREHKTLVQQLKEQNEALNRAhvQELLQCSERegalQEERADEAQQR----EEELR 831
Cdd:PRK11281 28 RAASNGDLPTEADVQAQL----DALNKQKLLEAEDKLVQQDLEQT--LALLDKIDR----QKEETEQLKQQlaqaPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 832 ALQEELSQAKCSSEE-----------AQLEH--AELQEQLHRANTDTAELGIQVCALTVEKERVEEALACAVQELQDake 898
Cdd:PRK11281 98 QAQAELEALKDDNDEetretlstlslRQLESrlAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 899 aasreregLERQVAGLQQEKE----SLQEKLKAAKAAAGSLPGLQAQLAQAEQRAQSLQEAAHQELNTLKFQLSAEIMDY 974
Cdd:PRK11281 175 --------IRNLLKGGKVGGKalrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 975 QS-----RLKnageeckslrgQLEEQGRQLQAAEEAVE----KLKATQADMGEKLS 1021
Cdd:PRK11281 247 QEainskRLT-----------LSEKTVQEAQSQDEAARiqanPLVAQELEINLQLS 291
|
|
| FYVE_WDFY1 |
cd15756 |
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ... |
1129-1192 |
5.28e-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: 5.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1894925300 1129 RWLgdtEANHCLDCKREFSWMV-----------RRHHCRICGRIFCYYCCNNYVLSKHGG--KKERCCRACFQKLSE 1192
Cdd:cd15756 2 QWL---ESDSCQKCEQPFFWNIkqmwdtktlglRQHHCRKCGQAVCGKCSSKRSSYPIMGfeFQVRVCDSCFETIKD 75
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
689-803 |
5.34e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.80 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 689 ELRALESQCQQQTQLIEVLTAEKGQQgvgpptdNEARELAAQLALSQAQLEVHQGEVQRL----------QAQVVDLQAK 758
Cdd:COG1566 84 ALAQAEAQLAAAEAQLARLEAELGAE-------AEIAAAEAQLAAAQAQLDLAQRELERYqalykkgavsQQELDEARAA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1894925300 759 MRAALDDQDKVQSQLSMAEAVLREHKTLVQ---QLKEQNEALNRAHVQ 803
Cdd:COG1566 157 LDAAQAQLEAAQAQLAQAQAGLREEEELAAaqaQVAQAEAALAQAELN 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
543-685 |
6.86e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 543 EAWGKPEEEQRGLQEAQLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGKLQALQADYQALQQRESAIQGslAS 622
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA--AA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 623 LEAEQASIRHLGDQMEASLLAVRKAKEAMK---AQMAEKEAILQSKEGECQQLREEVEQCQQLAEA 685
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAAAAAKKAAAEAKKkaeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
721-894 |
6.87e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 721 DNEARELAAQLA-LSQAqLEVHQGEVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAvlrehktlvqqlkeqneALNR 799
Cdd:PRK09039 52 DSALDRLNSQIAeLADL-LSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAG-----------------AGAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 800 AhvqellqcSEREGALQEERADEAQQREEELRalQEELSQAKCSSEEAQLehAELQEQLHRANTDTAELGIQVCALtveK 879
Cdd:PRK09039 114 A--------EGRAGELAQELDSEKQVSARALA--QVELLNQQIAALRRQL--AALEAALDASEKRDRESQAKIADL---G 178
|
170
....*....|....*
gi 1894925300 880 ERVEEALACAVQELQ 894
Cdd:PRK09039 179 RRLNVALAQRVQELN 193
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
662-841 |
7.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 662 LQSKEGECQQLREEVEQCQQLAEARHRELRALESQCQQQTQLIEVLTAEKGQQgvgpptDNEARELAAQLALSQAQLEVH 741
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 742 QG--EVQRLQAQVVDLQAKMRAALDDQDKVQSQLSMAEAVLREHKTLVQQLKEQNEALNRAHVQELLQCSEREGALQEER 819
Cdd:COG1579 86 RNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
170 180
....*....|....*....|..
gi 1894925300 820 ADEAQQREEELRALQEELSQAK 841
Cdd:COG1579 166 EELAAKIPPELLALYERIRKRK 187
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
749-966 |
7.13e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 749 QAQVVD-LQAKMRAaLDDQDKVQSQLSMAEAVLREHKTLVQQLKEQ--NEALNRAHV----------QELLQCSERegaL 815
Cdd:PRK10929 43 QAEIVEaLQSALNW-LEERKGSLERAKQYQQVIDNFPKLSAELRQQlnNERDEPRSVppnmstdaleQEILQVSSQ---L 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 816 QEErADEAQQREEELRALQEELSQAKCSSEEAQLEHAELQEQLHRANTDTAELG-IQVCALTVE----KERVEEaLACAV 890
Cdd:PRK10929 119 LEK-SRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAqAQLTALQAEsaalKALVDE-LELAQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 891 ------QELQDAK-EAASREREGLERQVAGL--------QQEKESLQEKLKAAKAAAGSLP-GLQAQLAQAEQRAQSLQE 954
Cdd:PRK10929 197 lsannrQELARLRsELAKKRSQQLDAYLQALrnqlnsqrQREAERALESTELLAEQSGDLPkSIVAQFKINRELSQALNQ 276
|
250
....*....|..
gi 1894925300 955 AAhQELNTLKFQ 966
Cdd:PRK10929 277 QA-QRMDLIASQ 287
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
332-591 |
8.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 332 LAMAQQKADTASDTKGRQEpipsDAAQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKED----ARASLER 407
Cdd:COG4942 12 ALAAAAQADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaaLEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 408 LVKEMAPLQEELSgkgQEADQLWRRLQELLAHTSSWEEELAELRREKKQQQEEKELLEQEVRSLTRQLQFLETQLAQVSQ 487
Cdd:COG4942 88 LEKEIAELRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 488 HVSDLEEQKKQLIQDKDHLSQQVGMLERLagppgpelpvAGEKNEALVPVNSSLQEAwgkpEEEQRGLQEAQLDDTKVQE 567
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEAL----------KAERQKLLARLEKELAEL----AAELAELQQEAEELEALIA 230
|
250 260
....*....|....*....|....
gi 1894925300 568 GSQEEELRQANRELEKELQNVVGR 591
Cdd:COG4942 231 RLEAEAAAAAERTPAAGFAALKGK 254
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
200-438 |
8.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 200 DQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERERGRTAAEDnvrltclvaelqkqwEVTQATQNTVKELQTCL 279
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS---------------EEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 280 QGLELGAAEKEEDYHTALRRLESMLQPLAQELEatrdsldkkNQHLASFPGWLAMAQQKADTASDTKGRQEPipsdaaqE 359
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAELEAELAELSARYTPNHP-------D 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 360 MQELGEKLQALERE-RTKVEEVNRQQSAQLEQLVKELQLKEDARASLERLVKEMAPLQEELSGKGQEADQLWRRLQELLA 438
Cdd:COG3206 293 VIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
184-438 |
8.81e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 184 LNNEALEGFDEMRLELDQLEVREKQLRERMQQLDRENQELRAAVSQQGEQLQTERErgrtaaednvrltclvAELQKQWE 263
Cdd:COG5185 280 LNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETE----------------TGIQNLTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 264 VTQATQNTVKELQTclqglELGAAEKEEDYHTALRRLESMLQPLAQELEATRDSLDKKNQHlasfpgWLAMAQQKADTAS 343
Cdd:COG5185 344 EIEQGQESLTENLE-----AIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQN------QRGYAQEILATLE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 344 DTKGRQEpipsdaaQEMQELGEKLQALERERTKVEEVNRQQSAQLEQLVKELQLKEDARASlERLVKEMAPLQEELSGKG 423
Cdd:COG5185 413 DTLKAAD-------RQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLE-EAYDEINRSVRSKKEDLN 484
|
250
....*....|....*
gi 1894925300 424 QEADQLWRRLQELLA 438
Cdd:COG5185 485 EELTQIESRVSTLKA 499
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
479-696 |
9.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 479 ETQLAQVSQHVSDLEEQKKQLIQDKDHLSQQVGmlerlagppgpelpvagEKNEALVPVNSSLQEAwgkpeEEQRGLQEA 558
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE-----------------ELNEEYNELQAELEAL-----QAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894925300 559 QLDDTKVQEGSQEEELRQANRELEKELQNVVGRNQLLEGK--------LQALQADYQALQQRESAIQGSLASLEAEQASI 630
Cdd:COG3883 73 EIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894925300 631 RHLGDQMEASLLAVRKAKEAMKAQMAEKEAILQSKEGECQQLREEVEQCQQLAEARHRELRALESQ 696
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| |
