|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1428.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKPKGSVAVgvgcslyfpwrsrNKHVQPcidcweasnslaeglsalremrLLWGKGEL 260
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAV-------------PHPAVN----------------------PAVLIGEL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14911 126 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPD 420
Cdd:cd14911 206 QREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASF 500
Cdd:cd14911 286 NTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDE 580
Cdd:cd14911 366 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 581 ECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVVQI 660
Cdd:cd14911 446 ECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNI 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 661 WKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCN 740
Cdd:cd14911 526 WKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCN 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 741 GVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14911 606 GVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
101-809 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1280.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKPKGSVAVGvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwGKGEL 260
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGK-------------------------------------------KKGTL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd01377 118 EDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDV-KTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLP 419
Cdd:cd01377 198 LKEKLLLTGDpSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 420 DNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd01377 278 GTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQY 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG-GIMALL 578
Cdd:cd01377 357 FIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPNmGILSIL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 579 DEECWFPKATDKSFVEKLAAAHSMHPKFMK--TDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPF 656
Cdd:cd01377 437 DEECVFPKATDKTFVEKLYSNHLGKSKNFKkpKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPL 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 657 VVQIWKDAEIVGmaqqaltDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQ 736
Cdd:cd01377 517 VASLFKDYEESG-------GGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQ 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158285519 737 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd01377 590 LRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1133.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwRSRNKHVQPcidcweasnslaeglsalremrllwgkGEL 260
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSH-----------------KGRKDHNIP---------------------------GEL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14920 117 ERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPD 420
Cdd:cd14920 197 LKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASF 500
Cdd:cd14920 277 NTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMAL 577
Cdd:cd14920 357 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLAL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 578 LDEECWFPKATDKSFVEKLAAAHSMHPKFMKT-DFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPF 656
Cdd:cd14920 437 LDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 657 VVQIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPL 732
Cdd:cd14920 517 VAELWKDVDrIVGLDQVTgMTETAFGSayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 733 VLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14920 597 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
89-809 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1129.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 89 VEDMAELTCLNEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSML 168
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 169 QDREDQSILCTGESGAGKTENTKKVIQYLAYVAASKPKGSVavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsal 248
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 249 remrllwgkGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFH 328
Cdd:pfam00063 122 ---------GRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYH 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 329 IFYQLLAGASPEQRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTF 407
Cdd:pfam00063 193 IFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEF 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 408 KQERNSDQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRIN 487
Cdd:pfam00063 273 KKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRIN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 488 RSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDL 567
Cdd:pfam00063 353 KSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 568 ID-KPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVV 646
Cdd:pfam00063 432 IEkKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLV 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 647 SLLQASQDPFVVQIWKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAG 726
Cdd:pfam00063 512 SLLKSSSDPLLAELFPDYETAESAAANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAG 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 727 KIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKI 806
Cdd:pfam00063 592 VFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKI 671
|
...
gi 158285519 807 FFR 809
Cdd:pfam00063 672 FFR 674
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
886-1966 |
0e+00 |
|
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: 1067.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 886 TKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDL 965
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 966 ESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEER 1045
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1046 ANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVK 1125
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1126 REEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQE 1205
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1206 LRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSR 1285
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1286 QENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEE 1365
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1366 TRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQ 1445
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1446 IQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLS 1525
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1526 LTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEV 1605
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1606 NMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQA 1685
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1686 KKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLM 1765
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1766 IDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQETA 1845
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1846 LRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLD 1925
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 158285519 1926 EAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKL 1966
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1047.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAAS----KPKGSVAVGvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwg 256
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSfktkKDQSSIALS-------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 257 KGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG 336
Cdd:cd14932 117 HGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 337 ASPEQRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQA 416
Cdd:cd14932 197 AGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 417 TLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQ 496
Cdd:cd14932 277 SMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 497 GASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---G 573
Cdd:cd14932 357 GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppG 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 574 IMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMK-TDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQAS 652
Cdd:cd14932 437 ILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKpKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 653 QDPFVVQIWKDAE-IVGMAQQA-LTDTQFGA-RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKID 729
Cdd:cd14932 517 TDKFVSELWKDVDrIVGLDKVAgMGESLHGAfKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLA 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 730 APLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14932 597 HHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
82-821 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1031.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 82 NPPKFDKVEDMAELTCLNEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITD 161
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 162 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAYVAASKPKgsvavgvgcslyfpwrsrnkhvqpcidcweasnsl 241
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 242 aeglsalremrllwgKGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQA 321
Cdd:smart00242 126 ---------------VGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 322 KDERTFHIFYQLLAGASPEQRERFILDDVKTYPFLSNGGLP-VPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVL 400
Cdd:smart00242 191 KGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLtVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAIL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 401 LFGSMTFKQERNSDQATLPDNT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMF 479
Cdd:smart00242 271 HLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 480 KWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGl 559
Cdd:smart00242 351 DWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 560 DLQPTIDLI-DKPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNM 638
Cdd:smart00242 429 DNQDCIDLIeKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNK 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 639 DPLNENVVSLLQASQDPFVVQIWKDAEivgmaqqaltdtqfGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCII 718
Cdd:smart00242 509 DTLSDDLIELLQSSKNPLIASLFPSGV--------------SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIK 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 719 PNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNL 798
Cdd:smart00242 575 PNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDE 654
|
730 740
....*....|....*....|...
gi 158285519 799 YRIGQSKIFFRAGVLAHLEEERD 821
Cdd:smart00242 655 YQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 990.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKpKGSVAVGVgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgKGEL 260
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSH-KGKKDTSI-------------------------------------------TGEL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14921 117 EKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPD 420
Cdd:cd14921 197 MRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASF 500
Cdd:cd14921 277 NTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMAL 577
Cdd:cd14921 357 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLAL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 578 LDEECWFPKATDKSFVEKLAAAHSMHPKFMKT-DFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPF 656
Cdd:cd14921 437 LDEECWFPKATDKSFVEKLCTEQGNHPKFQKPkQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 657 VVQIWKDAE-IVGMAQQA-LTDTQF--GARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPL 732
Cdd:cd14921 517 VADLWKDVDrIVGLDQMAkMTESSLpsASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFL 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 733 VLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14921 597 VLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 980.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwrsRNKHVQpcidcweasnslaeglsalremrllwgkGEL 260
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSH-------------------KSKKDQ----------------------------GEL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14919 114 ERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEH 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPD 420
Cdd:cd14919 194 LKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASF 500
Cdd:cd14919 274 NTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMAL 577
Cdd:cd14919 354 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILAL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 578 LDEECWFPKATDKSFVEKLAAAHSMHPKFMK-TDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPF 656
Cdd:cd14919 434 LDEECWFPKATDKSFVEKVVQEQGTHPKFQKpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKF 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 657 VVQIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPL 732
Cdd:cd14919 514 VSELWKDVDrIIGLDQVAgMSETALpGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHL 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 733 VLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14919 594 VLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 978.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASkPKGSVAVGVgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgKGEL 260
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGV-------------------------------------------PGEL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14930 117 ERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGvDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPD 420
Cdd:cd14930 197 LKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASF 500
Cdd:cd14930 276 NTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMAL 577
Cdd:cd14930 356 LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLAL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 578 LDEECWFPKATDKSFVEKLAAAHSMHPKFMKT-DFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPF 656
Cdd:cd14930 436 LDEECWFPKATDKSFVEKVAQEQGGHPKFQRPrHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 657 VVQIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 734
Cdd:cd14930 516 TAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVL 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 735 DQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14930 596 DQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-809 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 973.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwrsRNKHVQPcidcweasnslaeglsalremRLLWGKGEL 260
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSH-------------------KTKKDQN---------------------SLALSHGEL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd15896 121 EKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPD 420
Cdd:cd15896 201 LRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASF 500
Cdd:cd15896 281 NTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMAL 577
Cdd:cd15896 361 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILAL 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 578 LDEECWFPKATDKSFVEKLAAAHSMHPKFMK-TDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPF 656
Cdd:cd15896 441 LDEECWFPKATDKSFVEKVLQEQGTHPKFFKpKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKF 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 657 VVQIWKDAE-IVGMAQQALTDTQFGA-RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 734
Cdd:cd15896 521 VSELWKDVDrIVGLDKVSGMSEMPGAfKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 600
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 735 DQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd15896 601 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
38-1572 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 867.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 38 VWVPHESQGFVAASIKGERGDEVEVELA---ETGKRVLVLKDDIQ--KMNPPKFDKVEDMAELTCLNEASVLHNIKDRYY 112
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 113 SGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGESGAGKTENTKK 192
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 193 VIQYLAYVAASKPKGSVAVgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkgelEQQLLQANPILE 272
Cdd:COG5022 172 IMQYLASVTSSSTVEISSI-------------------------------------------------EKQILATNPILE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 273 AFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQRERFILDDVKT 352
Cdd:COG5022 203 AFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 353 YPFLSNGGLP-VPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNsDQATLPDNTVAQKIAHLL 431
Cdd:COG5022 283 YIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 432 GLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGaSFIGILDMAGFEI 511
Cdd:COG5022 362 GIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 512 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDK--PGGIMALLDEECWFPKATD 589
Cdd:COG5022 441 FEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATD 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 590 KSFVEKLAAA--HSMHPKFMKTDFRGVAdFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVVQIWKDAEiv 667
Cdd:COG5022 520 ESFTSKLAQRlnKNSNPKFKKSRFRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE-- 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 668 gmaqqaltdtqfgARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIR 747
Cdd:COG5022 597 -------------NIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIR 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 748 ICRQGFPNRIPFQEFRQRYELLTPNV----IPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFRAGVLAHLEEERDYK 823
Cdd:COG5022 664 ISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAK 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 824 ITDLIVNFQAFCRGFLARRNYQKRLQQLNAIRIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKedeLRQIR 903
Cdd:COG5022 744 LDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSY---LACII 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 904 DKlenlsKNSQEYEKKYQQAMEEKT-HLAEQLQAEIELCAEAEEgRARLVARKQELEE---LMQDLESRIEEEEERVNAL 979
Cdd:COG5022 821 KL-----QKTIKREKKLRETEEVEFsLKAEVLIQKFGRSLKAKK-RFSLLKKETIYLQsaqRVELAERQLQELKIDVKSI 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 980 TSEKkklQINIQDLEEQLEEEEAARQKLQLE---KVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEerANDLSQTLAEE 1056
Cdd:COG5022 895 SSLK---LVNLELESEIIELKKSLSSDLIENlefKTELIARLKKLLNNIDLEEGPSIEYVKLPELNK--LHEVESKLKET 969
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1057 EEKAKHLAKlkvKHESTIAELeerllkdHQQRQEADRSKRKIeTEVADLKEQINERRMQIEEMQQQLVKReeelaQTLVR 1136
Cdd:COG5022 970 SEEYEDLLK---KSTILVREG-------NKANSELKNFKKEL-AELSKQYGALQESTKQLKELPVEVAEL-----QSASK 1033
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1137 IDeesaakaaaqKTQRELESQLAEIQEdleaeklARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVAT 1216
Cdd:COG5022 1034 II----------SSESTELSILKPLQK-------LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTI 1096
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1217 LKKTLEDESANHESTLMDMRHKHAQEISSINEQ--LENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKq 1294
Cdd:COG5022 1097 NVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQeiSKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFA- 1175
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1295 AETQIAELQVKLadVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSS 1374
Cdd:COG5022 1176 ALSEKRLYQSAL--YDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTP 1253
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1375 KLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMK----------------KRSEEDSDIAKELEESKKkmNKD 1438
Cdd:COG5022 1254 ASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINvglfnalrtkasslrwKSATEVNYNSEELDDWCR--EFE 1331
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1439 IETLQRQIQELQAANdrldKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREARE 1518
Cdd:COG5022 1332 ISDVDEELEELIQAV----KVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPKEILKKIEALLIKQEL 1407
|
1530 1540 1550 1560 1570
....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 1519 KETkvLSLTRELDEAFEKIDELETKRKGLQNEL----DELANTQGTADKNVHELEKAK 1572
Cdd:COG5022 1408 QLS--LEGKDETEVHLSEIFSEEKSLISLDRNSiykeEVLSSLSALLTKEKIALLDRK 1463
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
101-809 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 841.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRH-EVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAYVAASKPKGSVAvgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwGKGE 259
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSS---------------------------------------------SASS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd00124 116 IEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFL-----SNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNS- 413
Cdd:cd00124 196 GAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDe 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 414 -DQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDR 492
Cdd:cd00124 276 dSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 493 TKRQ-GASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-K 570
Cdd:cd00124 356 TDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 571 PGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQ 650
Cdd:cd00124 435 PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLR 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 651 ASqdpfvvqiwkdaeivgmaqqaltdTQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDA 730
Cdd:cd00124 515 SG------------------------SQF----------------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDP 554
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 731 PLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd00124 555 ELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 772.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAAskpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnsLAEGLSALREMRLLWGKGEL 260
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAA--------------------------------------LGDGPGKKAQFLATKTGGTL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14927 123 EDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILD-DVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLP 419
Cdd:cd14927 203 LQDMLLVSmNPYDYHFCSQGVTTVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 420 DNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14927 283 GTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14927 362 FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAH-SMHPKFMK----TDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQD 654
Cdd:cd14927 442 EECMFPKASDASFKAKLYDNHlGKSPNFQKprpdKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQN 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 655 PFVVQIWKDaeIVGMAQQALTDTQFGARTRKGM-FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14927 522 KLLATLYEN--YVGSDSTEDPKSGVKEKRKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLV 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPK-GFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14927 600 LHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
102-809 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 771.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaeGLSALREMRLlwgKGELE 261
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATG---------------------------------------DLAKKKDSKM---KGTLE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14913 120 DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERF-ILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPD 420
Cdd:cd14913 200 IELLlITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14913 279 GTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQH 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14913 358 FIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKL------AAAHSMHPKFMKTdfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14913 438 EECMFPKATDTSFKNKLydqhlgKSNNFQKPKVVKG--RAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDAEivgmAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14913 516 NRLLAHLYATFA----TADADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14913 592 LHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 765.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKPKGSVAVGvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgKGEL 260
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKS--------------------------------------------KGSL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14909 117 EDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFIL-DDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLP 419
Cdd:cd14909 197 VKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 420 DNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14909 277 GEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14909 356 FIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAH-SMHPKFMKTD----FRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQD 654
Cdd:cd14909 436 EESMFPKATDQTFSEKLTNTHlGKSAPFQKPKppkpGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQN 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 655 PFVVQIWKDAEivgmAQQALTDTQFGARTRKGM-FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14909 516 KLLIEIFADHA----GQSGGGEQAKGGRGKKGGgFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIpKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14909 592 MHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 741.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKPKGSVavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwGKGEL 260
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSD----------------------------------------------GKGSL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14934 115 EDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFIL-DDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLP 419
Cdd:cd14934 195 LIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 420 DNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14934 275 TTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14934 354 FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAH-SMHPKFMKTDF-RGV---ADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQD 654
Cdd:cd14934 434 EQCVFPKATDATFKAALYDNHlGKSSNFLKPKGgKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 655 PFVVQIWKDAEIVGMAQQaltdtqfgaRTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 734
Cdd:cd14934 514 GLLALLFKEEEAPAGSKK---------QKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIM 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 735 DQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14934 585 HQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
101-809 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 714.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAA-SKPKGSVavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkGE 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAmIESKKKL------------------------------------------------GA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd14929 113 LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLP 419
Cdd:cd14929 193 LRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEAD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 420 DNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14929 273 GTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14929 352 FIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKL------AAAHSMHPKFMKTDFRgvADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14929 432 EECMFPKATDLTFKTKLfdnhfgKSVHFQKPKPDKKKFE--AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDAEIVGMAqqaltdTQFGARTRK--GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAP 731
Cdd:cd14929 510 NRLLASLFENYISTDSA------IQFGEKKRKkgASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPY 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 732 LVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14929 584 LVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
102-809 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 709.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAAskpkgsvavgVGcslyfpwrSRNKHVQPCidcweasnslaeglsalremrllwGKGELE 261
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAA----------IG--------DRSKKDQTP------------------------GKGTLE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14917 120 DQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFIL-DDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPD 420
Cdd:cd14917 200 LDMLLItNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTV-AQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14917 279 GTEeADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14917 358 FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKL------AAAHSMHPKFMKTdfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14917 438 EECMFPKATDMTFKAKLfdnhlgKSNNFQKPRNIKG--KPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDAEivgmAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14917 516 LKLLSNLFANYA----GADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14917 592 MHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
102-809 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 692.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKPKGSVavgvgcslyfpwrsrnkhvqpcidcwEASNSlaeglsalremrllwGKGELE 261
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKK--------------------------ENPNA---------------NKGTLE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14916 121 DQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPEL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFIL-DDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPD 420
Cdd:cd14916 201 LDMLLVtNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTV-AQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14916 280 GTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14916 359 FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKL------AAAHSMHPKFMKTdfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14916 439 EECMFPKASDMTFKAKLydnhlgKSNNFQKPRNVKG--KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDaeiVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14916 517 LKLMATLFST---YASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLV 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14916 594 MHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
102-809 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 688.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKPKGSVAVGVGcslyfpwrsrnkHVQpcidcweasnslaeglsalremrllwgkGELE 261
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSG------------KMQ----------------------------GTLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14912 122 DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPEL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFILD-DVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPD 420
Cdd:cd14912 202 IEMLLITtNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14912 281 GTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14912 360 FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKL------AAAHSMHPKFMKTdfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14912 440 EECMFPKATDTSFKNKLyeqhlgKSANFQKPKVVKG--KAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSA 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDAEiVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14912 518 MKTLAYLFSGAQ-TAEGASAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELV 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14912 597 LHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-809 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 683.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKPKGSVAVGVGcslyfpwrsrnkHVQpcidcweasnslaeglsalremrllwgkGELE 261
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSG------------KMQ----------------------------GTLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14910 122 DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFILD-DVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPD 420
Cdd:cd14910 202 IEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14910 281 GTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14910 360 FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAH------SMHPKFMKTDFRgvADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14910 440 EECMFPKATDTSFKNKLYEQHlgksnnFQKPKPAKGKVE--AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDAEivgMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14910 518 MKTLALLFSGAA---AAEAEEGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELV 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14910 595 LHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
103-809 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 682.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 103 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGES 182
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 183 GAGKTENTKKVIQYLAYVAASKPKGSVAVGvgcslyfpwrsrnkhvqpcidcweasnslaeglsalrEMrllwgKGELEQ 262
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESG-------------------------------------KM-----QGTLED 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 263 QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQR 342
Cdd:cd14918 121 QIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 343 ERFILD-DVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPDN 421
Cdd:cd14918 201 EMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 422 T-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGASF 500
Cdd:cd14918 280 TeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDE 580
Cdd:cd14918 359 IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 581 ECWFPKATDKSFVEKL------AAAHSMHPKFMKTdfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQD 654
Cdd:cd14918 439 ECMFPKATDTSFKNKLydqhlgKSANFQKPKVVKG--KAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAM 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 655 PFVVQIWKDAEivgmAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 734
Cdd:cd14918 517 KTLASLFSTYA----SAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVL 592
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 735 DQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14918 593 HQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
102-809 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 679.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKPKgsvavgvgcslyfpwrsrNKHVQPcidcweasnslaeglsalREMrllwgKGELE 261
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDK------------------KKEQQP------------------GKM-----QGTLE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14923 121 DQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFILD-DVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPD 420
Cdd:cd14923 201 IDLLLIStNPFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14923 280 GTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14923 359 FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAH------SMHPKFMKTdfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14923 439 EECMFPKATDTSFKNKLYDQHlgksnnFQKPKPAKG--KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDaeIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14923 517 LKLLSFLFSN--YAGAEAGDSGGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLV 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14923 595 MHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
102-809 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 675.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSG-LIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASkpkgsvavgvgcslyfpwrsrnkhvqpciDCWEASnslaeglsalremrllwgkgeL 260
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS-----------------------------SSGETQ---------------------V 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd01380 112 EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLP-VPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLP 419
Cdd:cd01380 192 ELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 420 DNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGA- 498
Cdd:cd01380 272 DDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQh 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 499 SFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALL 578
Cdd:cd01380 352 SFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 579 DEECWFPKATDKSFVEKLAAAHSMHPK--FMKTDFRGVAdFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDpf 656
Cdd:cd01380 431 DEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA-FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN-- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 657 vvqiwkdaeivgmaqqaltdtqfgartRKgmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQ 736
Cdd:cd01380 508 ---------------------------RK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQ 557
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158285519 737 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGfMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd01380 558 LRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
102-809 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 670.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKPKGSVavgvgcslyfpwrsrnkhvqpcidcwEASNSLAEGlsalremrllwgkgELE 261
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE--------------------------EAASGKMQG--------------TLE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14915 122 DQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFILD-DVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATlPD 420
Cdd:cd14915 202 IEMLLITtNPYDFAFVSQGEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrTKRQGAS 499
Cdd:cd14915 281 GTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLD 579
Cdd:cd14915 360 FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAH------SMHPKFMKTdfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14915 440 EECMFPKATDTSFKNKLYEQHlgksnnFQKPKPAKG--KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSG 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDAEivgMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14915 518 MKTLAFLFSGGQ---TAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELV 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14915 595 LHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
102-809 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 652.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAaskpkgsvavgvgcslyfpwrsrNKHVQpcidcweasnslaeglsalremrllwgkgeLE 261
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVT-----------------------NNHSW------------------------------VE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGA--SP 339
Cdd:cd14883 109 QQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFLS-NGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQ-ERNSDQAT 417
Cdd:cd14883 189 ELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 418 LPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQG 497
Cdd:cd14883 269 VEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 498 aSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDK-PGGIMA 576
Cdd:cd14883 349 -RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILK 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 577 LLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVAD-FAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDP 655
Cdd:cd14883 427 LLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTeFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNK 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 656 FVVQIWK--DAEIVGMAQQALTDTQFGARTRKGMfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14883 507 FVKELFTypDLLALTGLSISLGGDTTSRGTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELV 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14883 586 LAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
102-809 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 641.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVaaskpkgsvavgvgcslyfpwrsrnkhvqpcidcweaSNSLAEGLSALREMrllwgkgele 261
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-------------------------------------SGGSESEVERVKDM---------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 qqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd01378 115 --LLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKqERNSDQATLPD 420
Cdd:cd01378 193 LQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFA-EDEEGNAAISD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAfLTPRI----KVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQ 496
Cdd:cd01378 272 TSVLDFVAYLLGVDPDQLEKA-LTHRTietgGGGRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 497 GASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIM 575
Cdd:cd01378 351 KKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIF 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 576 ALLDEECWFP-KATDKSFVEKLAAAHSMHPKFM--KTDFR-GVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQA 651
Cdd:cd01378 430 AILDDACLTAgDATDQTFLQKLNQLFSNHPHFEcpSGHFElRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 652 SQDPFVVQIWKDAEIvgmaqqaltdtqfgaRTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAP 731
Cdd:cd01378 510 SSNPFLRSLFPEGVD---------------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEE 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 732 LVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd01378 575 LVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
101-809 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 634.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAYVAASkpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnSLAEGLSalremrllwgkge 259
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGR------------------------------------AVTEGRS------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd01384 112 VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATL 418
Cdd:cd01384 192 EDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 419 PD---NTVAQKIAHLLGLNVTDMTKAfLTPRIKVGRD-FVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTK 494
Cdd:cd01384 272 KDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 495 RQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGG 573
Cdd:cd01384 351 NS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 574 IMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd01384 429 IIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK-LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASK 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFVVQIWKDAEivgmaqqaltdtqfGARTRKGM-FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPL 732
Cdd:cd01384 508 CPFVAGLFPPLP--------------REGTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENAN 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 733 VLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNViPKGFMDGKRACEQMIKSLELDSnlYRIGQSKIFFR 809
Cdd:cd01384 574 VLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
102-809 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 630.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKgiKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAAskpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwGKGELE 261
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG-----------------------------------------------------GSSGIE 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd01383 107 NEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPAL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPD 420
Cdd:cd01383 187 REKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASF 500
Cdd:cd01383 267 DEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRS 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLD 579
Cdd:cd01383 347 ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLD 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGvadFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLqASQDPFVVQ 659
Cdd:cd01383 426 EESNFPKATDLTFANKLKQHLKSNSCFKGERGGA---FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 660 IWkdAEIVGMAQQALTdTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRC 739
Cdd:cd01383 502 LF--ASKMLDASRKAL-PLTKASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRC 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 740 NGVLEGIRICRQGFPNRIPFQEFRQRYE-LLTPNVIPKGfmDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd01383 579 CGVLEVVRISRSGYPTRMTHQEFARRYGfLLPEDVSASQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-809 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 621.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAAskpkgsvavgvgcslyfpwrsrnKHvqpcidCWeasnslaeglsalremrllwgkgeL 260
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG-----------------------QH------SW------------------------I 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd01381 108 EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQ--ERNSDQAT 417
Cdd:cd01381 188 EKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 418 LPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQG 497
Cdd:cd01381 268 VRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 498 AS--FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGI 574
Cdd:cd01381 348 SSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 575 MALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQD 654
Cdd:cd01381 427 MSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKN 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 655 PFVVQIWKDaeivgmaqqaltDTQFGARTRKGMfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 734
Cdd:cd01381 507 KFLKQLFNE------------DISMGSETRKKS-PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCV 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 735 DQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd01381 574 RQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
101-809 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 564.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkGEL 260
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGST-----------------------------------------------------NGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14872 108 EQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPA 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERfiLDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQA--- 416
Cdd:cd14872 188 SRGG--WGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVsgs 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 417 TLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKV-GRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKR 495
Cdd:cd14872 266 TVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 496 QGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDK-PGGI 574
Cdd:cd14872 346 AKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 575 MALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGV-ADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQ 653
Cdd:cd14872 425 MLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSrTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSK 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 654 DPFvvqiwkdaeIVGMAQQALTDTQFGARTRKGMFRtvshlykEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14872 505 NKL---------IAVLFPPSEGDQKTSKVTLGGQFR-------KQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMS 568
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLtPNVIPKGFM-DGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14872 569 LEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
101-809 |
5.78e-179 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 558.02 E-value: 5.78e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLayvaaskpkgsvavgvgCSLYfpwrsrnkhvqpcidcweasnslaeGLSAlremrllwgkGE 259
Cdd:cd01382 81 GESGAGKTESTKYILRYL-----------------TESW-------------------------GSGA----------GP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd01382 109 IEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDdvktypflsngglpvPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNS------ 413
Cdd:cd01382 189 DLREKLLKD---------------PLLDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcn 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 414 -DQATLPDNTVAqkiAHLLGLNVTDM-----TKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRIN 487
Cdd:cd01382 254 vKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRIN 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 488 RSLDRTKrqGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDL 567
Cdd:cd01382 331 QCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 568 ID-KPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMK------TDFRGVAD---FAVVHYAGKVDYSATKWLMKN 637
Cdd:cd01382 408 IEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIprksklKIHRNLRDdegFLIRHFAGAVCYETAQFIEKN 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 638 MDPLNENVVSLLQASQDPFVVQIWKDAEIVGmaqqALTDTQFGartrKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCI 717
Cdd:cd01382 488 NDALHASLESLICESKDKFIRSLFESSTNNN----KDSKQKAG----KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCI 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 718 IPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKgfMDGKRACEQMIKSLELDSN 797
Cdd:cd01382 560 KPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNEN 637
|
730
....*....|..
gi 158285519 798 LYRIGQSKIFFR 809
Cdd:cd01382 638 DFKFGLTKVFFR 649
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-809 |
2.27e-174 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 545.89 E-value: 2.27e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAaskPKGSVAVgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkgel 260
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---QRRNNLV------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDaSGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd01387 109 TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTF--KQERNS-DQA 416
Cdd:cd01387 188 LRQKYGLQEAEKYFYLNQGGnCEIAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFhkRQLRHGqEGV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 417 TLPDNTVAQKIAHLLGLNVTDMTKAfLTPRIKVGR-DFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINrSLDRTKR 495
Cdd:cd01387 268 SVGSDAEIQWVAHLLQISPEGLQKA-LTFKVTETRrERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 496 QGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGI 574
Cdd:cd01387 346 QDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAFA-DNQPVINLIsKKPVGI 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 575 MALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFrGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQD 654
Cdd:cd01387 425 LHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM-PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRT 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 655 PFVVQIWKDaeivgMAQQALTDTQFGAR----TRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDA 730
Cdd:cd01387 504 RVVAHLFSS-----HRAQTDKAPPRLGKgrfvTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDM 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 731 PLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGfmDGKRACEQMIKSLE--LDSNLYRIGQSKIFF 808
Cdd:cd01387 579 DVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP--APGDMCVSLLSRLCtvTPKDMYRLGATKVFL 656
|
.
gi 158285519 809 R 809
Cdd:cd01387 657 R 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-809 |
5.23e-170 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 534.35 E-value: 5.23e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQ----DREDQS 175
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 176 ILCTGESGAGKTENTKKVIQYLAYVAASKPKGSVAVGvgcslyfpwrsrnkhvqpcidcweasNSLAEGLSALremrllw 255
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEG--------------------------EAASEAIEQT------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 256 gKGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLA 335
Cdd:cd14890 128 -LGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 336 GASPEQRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNS-- 413
Cdd:cd14890 207 GADEALRERLKLQTPVEYFYLRGECSSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTtv 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 414 --DQATLPDntvAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLD 491
Cdd:cd14890 287 leDATTLQS---LKLAAELLGVNEDALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 492 RTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-K 570
Cdd:cd14890 364 SPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgK 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 571 PGGIMALLD--EECWFPKAT--DKSFVEKLAAAH-------------SMHPKFMKTDFRGVADFAVVHYAGKVDYSATKW 633
Cdd:cd14890 442 VNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFgrksgsggtrrgsSQHPHFVHPKFDADKQFGIKHYAGDVIYDASGF 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 634 LMKNMDPLNENVVSLLQASQdpfvvqiwkdaeivgmaqqaltdtqfgaRTRKGMfrTVSHLYKEQLAKLMDTLRNTNPNF 713
Cdd:cd14890 522 NEKNNETLNAEMKELIKQSR----------------------------RSIREV--SVGAQFRTQLQELMAKISLTNPRY 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 714 VRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVipkgfMDGKRACEQMIKSLE 793
Cdd:cd14890 572 VRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLG 646
|
730
....*....|....*.
gi 158285519 794 LDSNLYRIGQSKIFFR 809
Cdd:cd14890 647 LGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
101-807 |
1.67e-169 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 532.83 E-value: 1.67e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKY------KGIKRHEVPPHVFAITDTAYRSMLQDRE-- 172
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 173 --DQSILCTGESGAGKTENTKKVIQYLAYVAASKPKGSVAVgvgcslyfpwrsrnkhvqpcidcwEASNslaeglsalre 250
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNAT------------------------EREN----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 251 mrllwgkgeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIF 330
Cdd:cd14901 126 ---------VRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 331 YQLLAGASPEQRERFILDDVKTYPFLSNGGLPV--PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTF- 407
Cdd:cd14901 197 YELLRGASSDELHALGLTHVEEYKYLNSSQCYDrrDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFv 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 408 KQERNSDQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRIN 487
Cdd:cd14901 277 KKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRIN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 488 RSLDRTKRQGAS-FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgldlqPTID 566
Cdd:cd14901 357 ESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PNND 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 567 LI-----DKPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDF-RGVADFAVVHYAGKVDYSATKWLMKNMDP 640
Cdd:cd14901 432 ACvamfeARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFSVSKLqQGKRQFVIHHYAGAVCYATDGFCDKNKDH 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 641 LNENVVSLLQASQDPFVVQiwkdaeivgmaqqaltdtqfgartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPN 720
Cdd:cd14901 512 VHSEALALLRTSSNAFLSS------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPN 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 721 HEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNL-- 798
Cdd:cd14901 562 DVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIeh 641
|
730
....*....|..
gi 158285519 799 ---YRIGQSKIF 807
Cdd:cd14901 642 lppFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
101-809 |
1.48e-167 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 527.42 E-value: 1.48e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAYVAASKPKGSVavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkge 259
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDSTI-------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 leQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd14903 111 --KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EqrERFILDDVKTYPFL-SNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQATL 418
Cdd:cd14903 189 E--ERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 419 --PDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQ 496
Cdd:cd14903 267 iaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 497 gASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMA 576
Cdd:cd14903 347 -ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIIS 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 577 LLDEECWFPKATDKSFVEKLAAAH--SMH----PKFMKTdfrgvaDFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQ 650
Cdd:cd14903 425 LLNDEVMRPKGNEESFVSKLSSIHkdEQDviefPRTSRT------QFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMR 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 651 ASQDPFVVQIWKD-AEIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKID 729
Cdd:cd14903 499 GSSKPFLRMLFKEkVESPAAASTSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELD 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 730 APLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNViPKGFMDGKRACEQMIKSLELDS-NLYRIGQSKIFF 808
Cdd:cd14903 579 HLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYF 657
|
.
gi 158285519 809 R 809
Cdd:cd14903 658 Q 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
102-809 |
1.92e-162 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 512.59 E-value: 1.92e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwrSRNkhvqpcidcweasnslaeglsalremrllwgkgeLE 261
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKAN------------------NRT----------------------------------LE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd01379 110 EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 R-ERFILDDVKTYPFLSNGGLPVPGV---DDYAE-FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTF----KQERN 412
Cdd:cd01379 190 KlAKYKLPENKPPRYLQNDGLTVQDIvnnSGNREkFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 413 SDQATLPDNTVAQKIAHLLGLNVTDMTKAfLTPRIKVGR-DFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSL- 490
Cdd:cd01379 270 DKSSRISNPEALNNVAKLLGIEADELQEA-LTSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLk 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 491 -DRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTID-LI 568
Cdd:cd01379 349 pDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 569 DKPGGIMALLDEECWFPKATDKSFVEKLAaaHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSL 648
Cdd:cd01379 428 QKPMGLLALLDEESRFPKATDQTLVEKFH--NNIKSKYYWRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQL 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 649 LQASQDPFVVQiwkdaeivgmaqqaltdtqfgartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKI 728
Cdd:cd01379 506 LRSSENPLVRQ------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKF 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 729 DAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN----VIPKgfmdgKRACEQMIKSLELDSnlYRIGQS 804
Cdd:cd01379 556 DREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKwneeVVAN-----RENCRLILERLKLDN--WALGKT 628
|
....*
gi 158285519 805 KIFFR 809
Cdd:cd01379 629 KVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
101-809 |
1.16e-159 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 507.30 E-value: 1.16e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLayVAASKpKGSvAVGVgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkgel 260
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQ-KGY-GSGV----------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd01385 110 EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLS-NGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQER-NSDQATL 418
Cdd:cd01385 190 ERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 419 PDNT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSL----DRT 493
Cdd:cd01385 270 VGNPeVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 494 KRQGASfIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPG 572
Cdd:cd01385 350 EAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPT 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 573 GIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVAdFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQAS 652
Cdd:cd01385 428 GLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSS 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 653 Q----------DPFVVQIWKDAEIVGMAQQALTDTqfGARTRKG--------MFRTVSHL---------------YKEQL 699
Cdd:cd01385 507 SsafvreligiDPVAVFRWAVLRAFFRAMAAFREA--GRRRAQRtaghsltlHDRTTKSLlhlhkkkkppsvsaqFQTSL 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 700 AKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLtpnvIPKGFM 779
Cdd:cd01385 585 SKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLI 660
|
730 740 750
....*....|....*....|....*....|
gi 158285519 780 DGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd01385 661 SSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
101-809 |
4.49e-158 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 501.60 E-value: 4.49e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTE--KIMEKYKGIKRHEV-PPHVFAITDTAYRSMLQDR----ED 173
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSpPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 174 QSILCTGESGAGKTENTKKVIQYLAyvAASKPKGSVAVGVGcslyfpwrsrnkhvqpcidcweaSNSLAEglsalremrl 253
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLA--TASKLAKGASTSKG-----------------------AANAHE---------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 254 lwgkgELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQL 333
Cdd:cd14892 126 -----SIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 334 LAGASPEQRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTF----K 408
Cdd:cd14892 201 LAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFeenaD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 409 QERNSDQATLPDNTvaQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTK-AQTREQVEFAVEAIAKACYEKMFKWLVNRIN 487
Cdd:cd14892 281 DEDVFAQSADGVNV--AKAAGLLGVDAAELMFKLVTQTTSTARGSVLEiKLTAREAKNALDALCKYLYGELFDWLISRIN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 488 RSLDRTKRQ---------GASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFG 558
Cdd:cd14892 359 ACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 559 lDLQPTIDLIDK-PGGIMALLDEECWFP-KATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMK 636
Cdd:cd14892 439 -DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 637 NMDPLNENVVSLLQASqdpfvvqiwkdaeivgmaqqaltdtqfgartRKgmFRTvshlykeQLAKLMDTLRNTNPNFVRC 716
Cdd:cd14892 518 NNDNLHDDLRDLLRSS-------------------------------SK--FRT-------QLAELMEVLWSTTPSYIKC 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 717 IIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVI-------PKGFMDGKRACEQMI 789
Cdd:cd14892 558 IKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNKAgvaaspdACDATTARKKCEEIV 637
|
730 740
....*....|....*....|
gi 158285519 790 KSlELDSNLYRIGQSKIFFR 809
Cdd:cd14892 638 AR-ALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
101-809 |
1.67e-157 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 500.37 E-value: 1.67e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKgIKRHEVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAYVAaskpkgsvavgvgcslyfpwrsrnkhvqpcidcweaSNSLaeglsalrEMRLLwgkge 259
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAG------------------------------------SEDI--------KKRSL----- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD---------ASGYISGANIETYLLEKSRAIRQAKDERTFHIF 330
Cdd:cd14888 111 VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 331 YQLLAGASPEQRERFILDDVKTYPFLSNGGLPV------------------------PGVDDYAEFQATVKSMNIMGMTS 386
Cdd:cd14888 191 YQLCAAAREAKNTGLSYEENDEKLAKGADAKPIsidmssfephlkfryltksschelPDVDDLEEFESTLYAMQTVGISP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 387 EDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPDNTVAQ---KIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQV 463
Cdd:cd14888 271 EEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 464 EFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 543
Cdd:cd14888 351 EDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEK 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 544 EYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFM--KTDfrgVADFAVV 620
Cdd:cd14888 431 LYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDvvKTD---PNSFVIV 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 621 HYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVVQIWKdaeivgmaqqALTDTQFGARTRKGMFRTVSHLYKEQLA 700
Cdd:cd14888 507 HFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS----------AYLRRGTDGNTKKKKFVTVSSEFRNQLD 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 701 KLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvipkgfmd 780
Cdd:cd14888 577 VLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN--------- 647
|
730 740
....*....|....*....|....*....
gi 158285519 781 gkracEQMIKSLEldsnLYRIGQSKIFFR 809
Cdd:cd14888 648 -----GEGKKQLS----IWAVGKTLCFFK 667
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
101-809 |
3.17e-157 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 498.45 E-value: 3.17e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKG-IKRHEVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNlSVRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgKGE 259
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD----------------------------------------------------DSD 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd14897 109 LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFLSNGGLPVPGVDDYAE-------FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERN 412
Cdd:cd14897 189 DRLLYYFLEDPDCHRILRDDNRNRPVFNDSEEleyyrqmFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDED 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 413 SDQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSL-- 490
Cdd:cd14897 269 TDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwp 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 491 --DRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI 568
Cdd:cd14897 349 dkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 569 -DKPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTdFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVS 647
Cdd:cd14897 428 fKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS-PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVG 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 648 LLQASQDPFVvqiwkdaeivgmaqqaltdtqfgartrKGMFrtVSHlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGK 727
Cdd:cd14897 507 CLLNSNNEFI---------------------------SDLF--TSY-FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNK 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 728 IDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNViPKGFMDGKRACEQMIKSLELDSnlYRIGQSKIF 807
Cdd:cd14897 557 FDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVF 633
|
..
gi 158285519 808 FR 809
Cdd:cd14897 634 LK 635
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-809 |
7.01e-156 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 495.47 E-value: 7.01e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAYVAASkpkgsvavgvgcSLYFPWRSRNKHVqpcidcweasnslaeglsalremrllwgkge 259
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQ------------SLELSLKEKTSCV------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 lEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd14873 118 -EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEH 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKqerNSDQATL 418
Cdd:cd14873 197 EEREEFYLSTPENYHYLNQSGcVEDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 419 PDNTVAQKIAHLLGLNVTDMTKAfLTPRIKVGR-DFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLdrTKRQG 497
Cdd:cd14873 274 SFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKED 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 498 ASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMAL 577
Cdd:cd14873 351 FKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLAL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 578 LDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFrGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFV 657
Cdd:cd14873 430 INEESHFPQATDSTLLEKLHSQHANNHFYVKPRV-AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFI 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 658 VQIWkdaEIVGMAQQalTDTQFGARTRKGmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQL 737
Cdd:cd14873 509 YDLF---EHVSSRNN--QDTLKCGSKHRR--PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQL 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 738 RCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKraCEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14873 582 RYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
103-809 |
1.73e-146 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 469.77 E-value: 1.73e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 103 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSML----QDREDQSILC 178
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 179 TGESGAGKTENTKKVIQYLayvaaskpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalreMRLLWGKG 258
Cdd:cd14889 83 SGESGAGKTESTKLLLRQI-----------------------------------------------------MELCRGNS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 259 ELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAS 338
Cdd:cd14889 110 QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGIS 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 339 PEQRERFILDDVKTYPFLSNGGLPVPGVDDY-AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFK-QERNSDQA 416
Cdd:cd14889 189 AEDRENYGLLDPGKYRYLNNGAGCKREVQYWkKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEmDDDEALKV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 417 TLPDNTVAQKIAHLLGLNVTDMTKAfLTPRIKVGR-DFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKR 495
Cdd:cd14889 269 ENDSNGWLKAAAGQFGVSEEDLLKT-LTCTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 496 QG--ASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDL-IDKPG 572
Cdd:cd14889 348 SSveLREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 573 GIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFmKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVV-----S 647
Cdd:cd14889 427 GILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY-GKSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRtlfinS 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 648 LLQASQDPFVVQIWKDAEIVGMAQQALTDTQFGARTRKgmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGK 727
Cdd:cd14889 506 ATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQ 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 728 IDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLtpnVIPKGFMDGKRACEQMIKSLELDSnlYRIGQSKIF 807
Cdd:cd14889 583 LDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL---LCEPALPGTKQSCLRILKATKLVG--WKCGKTRLF 657
|
..
gi 158285519 808 FR 809
Cdd:cd14889 658 FK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-774 |
1.69e-145 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 467.20 E-value: 1.69e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRH--------EVPPHVFAITDTAYRSMLQDR 171
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 172 EDQSILCTGESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwRSRNKHVQPcidcweASNSLAEGLSalrem 251
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQE-----------------QNSEEVLTL------TSSIRATSKS----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 252 rllwgKGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-ASGYISGANIETYLLEKSRAIRQAKDERTFHIF 330
Cdd:cd14907 133 -----TKSIEQKILSCNPILEAFGNAKTVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 331 YQLLAGASPEQRERF-ILDDVKTYPFLS---NGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMT 406
Cdd:cd14907 208 YHLLYGADQQLLQQLgLKNQLSGDRYDYlkkSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 407 FKQER-NSDQATLPDNT-VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVN 484
Cdd:cd14907 288 FDDSTlDDNSPCCVKNKeTLQIIAKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 485 RINRSL-------DRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKF--I 555
Cdd:cd14907 368 RLNDTImpkdekdQQLFQNKYLSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 556 DFgLDLQPTIDLIDK-PGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWL 634
Cdd:cd14907 448 SY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFR 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 635 MKNMDPLNENVVSLLQASQDPFVVQIWKDAeivgmaQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFV 714
Cdd:cd14907 527 EKNKDEISQSIINCIQNSKNRIISSIFSGE------DGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFI 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 715 RCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVI 774
Cdd:cd14907 601 RCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKNVL 660
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-766 |
4.94e-140 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 450.53 E-value: 4.94e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKY-------------KGikRHEVPPHVFAITDTAYRSM 167
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 168 ----LQDREDQSILCTGESGAGKTENTKKVIQYLAYVAASKPKGSVAVGVGcslyfpwrsrnkhvqpcidcweasnslAE 243
Cdd:cd14900 80 mlglNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKS---------------------------TS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 244 GLSAlremrllwgkgeleqQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKD 323
Cdd:cd14900 133 GIAA---------------KVLQTNILLESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 324 ERTFHIFYQLLAGASPEQRERFIlddvktypflsngglpvpgvddyaeFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFG 403
Cdd:cd14900 198 ERNYHIFYEMAIGASEAARKRDM-------------------------YRRVMDAMDIIGFTPHERAGIFDLLAALLHIG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 404 SMTFKQERNSDQATLPDNTVAQK-------IAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYE 476
Cdd:cd14900 253 NLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 477 KMFKWLVNRIN---RSLDRTKRQGAS-FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEW 552
Cdd:cd14900 333 RLFDWLVGKMNaflKMDDSSKSHGGLhFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDW 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 553 KFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDF-RGVADFAVVHYAGKVDYSA 630
Cdd:cd14900 413 KYVEFC-DNQDCVNLISqRPTGILSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIqRARGLFTIVHYAGHVEYST 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 631 TKWLMKNMDPLNENVVSLLQasqdpfvvqiwkdaeivgmaqqalTDTQFgartrkgmfrtvshlyKEQLAKLMDTLRNTN 710
Cdd:cd14900 492 DGFLEKNKDVLHQEAVDLFV------------------------YGLQF----------------KEQLTTLLETLQQTN 531
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 711 PNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 766
Cdd:cd14900 532 PHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARY 587
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
101-809 |
6.16e-139 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 448.62 E-value: 6.16e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAYVAASKPKGSVAvgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkge 259
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA------------------------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 leqQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd14904 112 ---KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSS 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFL--SNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFkQERNSDQAT 417
Cdd:cd14904 189 EERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 418 LPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQG 497
Cdd:cd14904 268 ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 498 ASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDKPGGIMAL 577
Cdd:cd14904 348 KGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIAL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 578 LDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGV--ADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDP 655
Cdd:cd14904 427 MNDHLRQPRGTEEALVNKIRTNHQTKKDNESIDFPKVkrTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLD 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 656 FVVQIWKDAEivgmaqqaLTDTQFGARTRKGMF--RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLV 733
Cdd:cd14904 507 LLTELFGSSE--------APSETKEGKSGKGTKapKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMV 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 734 LDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGfmDGKRACEQMIKSLELDSNL-YRIGQSKIFFR 809
Cdd:cd14904 579 VEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
101-809 |
3.18e-136 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 442.04 E-value: 3.18e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYK--GIKRHE-------VPPHVFAITDTAYRSMLQD- 170
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 171 REDQSILCTGESGAGKTENTKKVIQYLAYVAASkpkGSVAVGVGCSLyfpwrsrnkhvqpcidcweasnslaeglsalre 250
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNG---EEGAPNEGEEL--------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 251 mrllwGKGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIF 330
Cdd:cd14908 125 -----GKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 331 YQLLAGASPEQRERFILDDVKT--------YPFLSNGGLP-VPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLL 401
Cdd:cd14908 200 YQLLRGGDEEEHEKYEFHDGITgglqlpneFHYTGQGGAPdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 402 FGSMTFKQERNSDQ---ATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKM 478
Cdd:cd14908 280 LGQLEFESKEEDGAaeiAEEGNEKCLARVAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGAL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 479 FKWLVNRINRSL--DRTKRQGASfIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFID 556
Cdd:cd14908 360 FLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 557 FGlDLQPTIDLID-KPGGIMALLDEECWFP-KATDKSFVEKL--------AAAHSMHPKFMKTDF-RGVADFAVVHYAGK 625
Cdd:cd14908 439 FP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRLyetylpekNQTHSENTRFEATSIqKTKLIFAVRHFAGQ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 626 VDYSA-TKWLMKNMDPLNENVVSLLQASQdpfvvqiwkdaeivgmaqqaltdtQFgartrkgmfrtvshlyKEQLAKLMD 704
Cdd:cd14908 518 VQYTVeTTFCEKNKDEIPLTADSLFESGQ------------------------QF----------------KAQLHSLIE 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 705 TLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP----NVIPKGFM- 779
Cdd:cd14908 558 MIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipeVVLSWSMEr 637
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 158285519 780 -DGKRACEQ--------------MIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14908 638 lDPQKLCVKkmckdlvkgvlspaMVSMKNIPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
101-809 |
1.81e-135 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 438.32 E-value: 1.81e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRyySGLI----YTYSGLFCVVVNPYKKLPiytEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDRE---D 173
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 174 QSILCTGESGAGKTENTKKVIQYLAYVAASKPKGSVAVGvgcslyfpwrsrnkhvqpcidcwEASNSLAEGLSAlremrl 253
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDI-----------------------EQSSKKRKLSVT------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 254 lwgkgELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGY-ISGANIETYLLEKSRAIRQAKDERTFHIFYQ 332
Cdd:cd14891 127 -----SLDERLMDTNPILESFGNAKTLRNHNSSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 333 LLAGASPEQRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQER 411
Cdd:cd14891 202 LLAGASAELLKELLLLSPEDFIYLNQSGcVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEED 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 412 NS----DQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIkVGRD--FVTKAQTREQVeFAVEAIAKACYEKMFKWLVNR 485
Cdd:cd14891 282 TSegeaEIASESDKEALATAAELLGVDEEALEKVITQREI-VTRGetFTIKRNAREAV-YSRDAIAKSIYERLFLWIVQQ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 486 INRSLDRtKRQGASFIGILDMAGFEIFEL-NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPT 564
Cdd:cd14891 360 INTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNREC 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 565 IDLI-DKPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKT---DFRGVadFAVVHYAGKVDYSATKWLMKNMDP 640
Cdd:cd14891 438 LDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTHKRHPCFPRPhpkDMREM--FIVKHYAGTVSYTIGSFIDKNNDI 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 641 LNENVVSLLQASQdpfvvqiwkdaeivgmaqqaltdtqfgartrkgmfrtvshLYKEQLAKLMDTLRNTNPNFVRCIIPN 720
Cdd:cd14891 516 IPEDFEDLLASSA----------------------------------------KFSDQMQELVDTLEATRCNFIRCIKPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 721 HEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY-ELLTPNVIPKgFMDGKRA-CEQMIKSLELDSNL 798
Cdd:cd14891 556 AAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYkPVLPPSVTRL-FAENDRTlTQAILWAFRVPSDA 634
|
730
....*....|.
gi 158285519 799 YRIGQSKIFFR 809
Cdd:cd14891 635 YRLGRTRVFFR 645
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
99-851 |
2.15e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 433.30 E-value: 2.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 99 NEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHE-VPPHVFAITDTAYRSMLQDREDQSIL 177
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 178 CTGESGAGKTENTKKVIQYLAYvaaskpkgsvavGVGcslyfpwRSRNKHVQpcidcweasnslaeglsalremrllwgk 257
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFAS------------SKS-------GNMDLKIQ---------------------------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 258 geleQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGA 337
Cdd:PTZ00014 221 ----NAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 338 SPEQRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERN---SD 414
Cdd:PTZ00014 297 NDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgglTD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 415 QATLPDNT--VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDR 492
Cdd:PTZ00014 377 AAAISDESleVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEP 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 493 TKRQGAsFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKP 571
Cdd:PTZ00014 457 PGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKG 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 572 GGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQA 651
Cdd:PTZ00014 535 KSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKA 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 652 SQDPFVVQIWKDAEIV--GMAQQALTDTQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKID 729
Cdd:PTZ00014 615 SPNPLVRDLFEGVEVEkgKLAKGQLIGSQF----------------LNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWN 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 730 APLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:PTZ00014 679 SSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLK 758
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 158285519 810 ---AGVLAHLEEERDYKITDLIVNFQAFCRGFLARRNYQKRLQQL 851
Cdd:PTZ00014 759 kdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSL 803
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
101-771 |
6.51e-131 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 428.16 E-value: 6.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYK--------GIKRHEVPPHVFAITDTAYRSMLQ-D 170
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 171 REDQSILCTGESGAGKTENTKKVIQYLAYVAASKPKGSVavgvgcslyfpwrsrnkhvqpcidcwEASNSLaeglsalre 250
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQ--------------------------EGSDAV--------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 251 mrllwgkgELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIF 330
Cdd:cd14902 126 --------EIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 331 YQLLAGASPEQRERFILDDVKTYPFLSNGG-----LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSM 405
Cdd:cd14902 198 YELLEGADKTLLDLLGLQKGGKYELLNSYGpsfarKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 406 TFKQERNSDQATLPDNTVA---QKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWL 482
Cdd:cd14902 278 NFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 483 VNRINRSLD--------RTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKF 554
Cdd:cd14902 358 VRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKN 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 555 IDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKSFVEKLAAAHSmhpkfmktdfrGVADFAVVHYAGKVDYSATKWL 634
Cdd:cd14902 438 ISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKFYRYHG-----------GLGQFVVHHFAGRVCYNVEQFV 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 635 MKNMDPLNENVVSLLQASQDPFVVQIWKDAEIVGMAqqalTDTQFGARTRKGMFRT--VSHLYKEQLAKLMDTLRNTNPN 712
Cdd:cd14902 507 EKNTDALPADASDILSSSSNEVVVAIGADENRDSPG----ADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAH 582
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 713 FVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 771
Cdd:cd14902 583 YVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
101-807 |
4.99e-129 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 420.55 E-value: 4.99e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRH-EVPPHVFAITDTAYRSMLQDREDQSILCT 179
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAyvaaSKPKGSVavgvgcslyfpwrsrNKHVQPCIdcweasnslaeglsalremrllwgkge 259
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----SAKSGNM---------------DLRIQTAI--------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 leqqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASP 339
Cdd:cd14876 115 -----MAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 340 EQRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERN---SDQA 416
Cdd:cd14876 190 EMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEqgvDDAA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 417 TL--PDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDrtK 494
Cdd:cd14876 270 AIsnESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--P 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 495 RQG-ASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTID-LIDKPG 572
Cdd:cd14876 348 PGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGK 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 573 GIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQAS 652
Cdd:cd14876 427 SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQAS 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 653 QDPFVVQIWKDAEIVG--MAQQALTDTQFGArtrkgmfrtvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDA 730
Cdd:cd14876 507 TNPVVKALFEGVVVEKgkIAKGSLIGSQFLK----------------QLESLMGLINSTEPHFIRCIKPNETKKPLEWNS 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 731 PLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIF 807
Cdd:cd14876 571 SKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
101-809 |
9.12e-128 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 416.87 E-value: 9.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAyvaaskpkgsvavgvgcSLYfPWRSRNKHVQPCidcweasNSLaeglsalremrllwgkgel 260
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLS-----------------SLY-QDQTEDRLRQPE-------DVL------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 eqqllqanPILEAFGNAKTVKNDNSSRFGKFIRINFDaSGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14896 117 --------PILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGL-PVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQ-ERNSDQ-AT 417
Cdd:cd14896 188 EREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSsERESQEvAA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 418 LPDNTVAQKIAHLLGLNvTDMTKAFLTPRIKV---GRDFvtkaqTREQVEFAVEA---IAKACYEKMFKWLVNRINRSLD 491
Cdd:cd14896 268 VSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtpyGRVS-----RPLPVEGAIDArdaLAKTLYSRLFTWLLKRINAWLA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 492 RTKRQGA-SFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDfGLDLQPTIDLI-D 569
Cdd:cd14896 342 PPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvD 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 570 KPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRgVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLL 649
Cdd:cd14896 421 QPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLP-LPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEML 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 650 QASQDPFVVQIWKDAEivgmaqqaltdTQFGARTRKGmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKID 729
Cdd:cd14896 500 AQSQLQLVGSLFQEAE-----------PQYGLGQGKP---TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFD 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 730 APLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTpNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd14896 566 VGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
101-809 |
1.17e-122 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 404.00 E-value: 1.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASkPKGSVAVgvgcslyfpwrsrnkhvqpcidcweasnslaEGLSAlremrllwgkgel 260
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGS-VGGVLSV-------------------------------EKLNA------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 eqqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd01386 116 ------ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTypflSNGGLPVPGV------DDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSD 414
Cdd:cd01386 190 LRTELHLNQLAE----SNSFGIVPLQkpedkqKAAAAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 415 QATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQ-------------VEfAVEAIAKACYEKMFKW 481
Cdd:cd01386 266 RKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESparsssggpkltgVE-ALEGFAAGLYSELFAA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 482 LVNRINRSLDRTKRQGASfIGILDMAGFEIFELN------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfI 555
Cdd:cd01386 345 VVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---V 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 556 DFGLD---LQPTIDLIDK---------------PGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVAD- 616
Cdd:cd01386 421 DFDLPelsPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEg 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 617 ---FAVVHYAGK--VDYSATKWLMK-NMDPLNENVVSLLQASQDpfvvqiwkdaeivgmaqqaltdtQFGARTRKGMFRT 690
Cdd:cd01386 501 plqFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQK-----------------------ETAAVKRKSPCLQ 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 691 VshlyKEQLAKLMDTLRNTNPNFVRCIIPNH--EKRAGK----------IDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 758
Cdd:cd01386 558 I----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMP 633
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 759 FQEFRQRYELLTPNVIPKGF-----MDGKRACEQMIKSLELDSNLYRIGQSKIFFR 809
Cdd:cd01386 634 LGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
102-770 |
4.25e-119 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 394.32 E-value: 4.25e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTekiMEKYKGIKRH--EVPPHVFAITDTAYRSMLQ-------DR 171
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGwtALPPHVFSIAEGAYRSLRRrlhepgaSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 172 EDQSILCTGESGAGKTENTKKVIQYLAYVAASKPKGSvavgvgcslyfpwrsrnkhvqpcidcwEASNSLAEGLSalrem 251
Cdd:cd14895 79 KNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATS---------------------------SSKRRRAISGS----- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 252 rllwgkgeleqQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-----DASGYISGANIETYLLEKSRAIRQAKDERT 326
Cdd:cd14895 127 -----------ELLSANPILESFGNARTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 327 FHIFYQLLAGASPEQRERFILDDV--KTYPFLSNGGLPV--PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLF 402
Cdd:cd14895 196 FHVFYELLAGAADDMKLELQLELLsaQEFQYISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 403 GSMTFKQERNSD---------------QATLPDNTVAQK---IAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVE 464
Cdd:cd14895 276 GNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQHldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 465 FAVEAIAKACYEKMFKWLVNRINRSLDRTK----------RQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 534
Cdd:cd14895 356 DARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 535 HTMFILEQEEYQREGIEWKFIDFGLDlQPTIDLID-KPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFM--KTDF 611
Cdd:cd14895 436 QDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSasRTDQ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 612 RGVAdFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVVQIWKDAEIVGMAQQALTdtQFGARTRKGMFRTV 691
Cdd:cd14895 515 ADVA-FQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLG--QPKLRRRSSVLSSV 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 692 S--HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 769
Cdd:cd14895 592 GigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL 671
|
.
gi 158285519 770 T 770
Cdd:cd14895 672 V 672
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
101-771 |
7.02e-116 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 383.43 E-value: 7.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKR-HEVPPHVFAITDTAYRSMLQDRE--DQSI 176
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 177 LCTGESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgCSlyfpwrsrnkhvqpcidcWEaSNSLAEglsalremrllwg 256
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP----------TS------------------WE-SHKIAE------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 257 kgELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG 336
Cdd:cd14880 119 --RIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 337 ASPEQRERFILDDVKTYPFLSNgglPVPGVDDyAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQA 416
Cdd:cd14880 197 ASADERLQWHLPEGAAFSWLPN---PERNLEE-DCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 417 TLPDNTV---AQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVT--KAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLD 491
Cdd:cd14880 273 CQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSIC 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 492 RTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-K 570
Cdd:cd14880 353 ADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgS 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 571 PGGIMALLDEECWFPKATDKS-FVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLL 649
Cdd:cd14880 432 PISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 650 QASQDPFVVQIWKDAEivgmaqQALTDTQFGARTRKGMFRTVSHlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKID 729
Cdd:cd14880 512 QQSQDPLLQKLFPANP------EEKTQEEPSGQSRAPVLTVVSK-FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFL 584
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 158285519 730 APLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 771
Cdd:cd14880 585 QEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
101-809 |
6.52e-113 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 374.92 E-value: 6.52e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYS-GLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGI-KRHEVPPHVFAITDTAYRSM-LQDREDQSIL 177
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 178 CTGESGAGKTENTKKVIQYLAYVAaskpkgsvavgvgcslyfpwrsrnkhvqpcidCWEASNSLAEGLSALREMRLLWgk 257
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLS--------------------------------YMHSSNTSQRSIADKIDENLKW-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 258 geleqqllqANPILEAFGNAKTVKNDNSSRFGKFIRINFD-ASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG 336
Cdd:cd14875 127 ---------SNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 337 ASPEQRERfiLDDVKT---YPFLSNGGLPVP-GVD-----DYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTF 407
Cdd:cd14875 198 LSPEEKKE--LGGLKTaqdYKCLNGGNTFVRrGVDgktldDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 408 KQERNsDQATLPDNTVAQKIAHLLGLNVTDMTKAFLtprIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRIN 487
Cdd:cd14875 276 ESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVN 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 488 RSLD-RTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTID 566
Cdd:cd14875 352 ASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 567 LID-KPGGIMALLDEECWFPKATDKSFVEKL-AAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNEN 644
Cdd:cd14875 431 MFDqKRTGIFSMLDEECNFKGGTTERFTTNLwDQWANKSPYFVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKED 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 645 VVSLLQASQDPFVvqiwkdaeivgmaqQALTDTQFGARTRKgmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKR 724
Cdd:cd14875 511 MYECVSNSTDEFI--------------RTLLSTEKGLARRK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEAS 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 725 AGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFmdgKRAC--EQMIKSLELDSNLYR-- 800
Cdd:cd14875 574 PSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLF---KQEKysEAAKDFLAYYQRLYGwa 650
|
730
....*....|....
gi 158285519 801 -----IGQSKIFFR 809
Cdd:cd14875 651 kpnyaVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
101-805 |
2.75e-110 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 369.31 E-value: 2.75e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKR-HEVPPHVFAITDTAYRSMLQDREDQSILC 178
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 179 TGESGAGKTENTKKVIQYLAYVAASKPKGSVAVGvgcslyfpwRSRNKhvqpcidcweasnslaeglsalremrllwgkg 258
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNN---------NNNNS-------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 259 eLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS-GYISGANIETYLLEKSR-AIRQAKDERTFHIFYQLLAG 336
Cdd:cd14906 120 -IEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 337 ASPEQRERFILD-DVKTYPFL--------------SNGGLPVPGVDDYAE-FQATVKSMNIMGMTSEDFNSIFRIVSAVL 400
Cdd:cd14906 199 ASKDERSKWGLNnDPSKYRYLdarddvissfksqsSNKNSNHNNKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAIL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 401 LFGSMTFKQERN-SDQATLPDNTVA--QKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTRE--QVEFAVEAIAKACY 475
Cdd:cd14906 279 HLGNIEFEEDSDfSKYAYQKDKVTAslESVSKLLGYIESVFKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 476 EKMFKWLVNRINRSLDR----------TKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 545
Cdd:cd14906 359 VRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEY 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 546 QREGIEWKFIDFgLDLQPTIDLIDKPG-GIMALLDEECWFPKATDKSFVEKLAAA-HSMHPKFMKTDFRGVadFAVVHYA 623
Cdd:cd14906 439 LSEGIPWSNSNF-IDNKECIELIEKKSdGILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQRTLAKGT--LGIKHFA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 624 GKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVVQIWKdaeivgmaQQALTDTQFGARTRKGMfrTVSHLYKEQLAKLM 703
Cdd:cd14906 516 GDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ--------QQITSTTNTTKKQTQSN--TVSGQFLEQLNQLI 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 704 DTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKR 783
Cdd:cd14906 586 QTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKL 665
|
730 740
....*....|....*....|..
gi 158285519 784 ACEQMIKSLELDSNLYRIGQSK 805
Cdd:cd14906 666 ASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
101-809 |
7.61e-109 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 363.05 E-value: 7.61e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKG--IKR---HEVPPHVFAITDTAYRSMLQDREDQ 174
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQadTSRgfpSDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 175 SILCTGESGAGKTENTKKVIQYLAYVAASkpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrll 254
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 255 wGKGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLL 334
Cdd:cd14886 110 -SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCI 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 335 AGASPEQRERFILDDVKTYPFLsNGG--LPVPGVDDYAEFQATVKSMNIMgMTSEDFNSIFRIVSAVLLFGSMTFKQERN 412
Cdd:cd14886 189 KGLSPEEKKSLGFKSLESYNFL-NASkcYDAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 413 S---DQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINR- 488
Cdd:cd14886 267 MgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEi 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 489 -SLDRTKRQgasFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDL 567
Cdd:cd14886 347 iQFDADARP---WIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAV 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 568 IDKPG-GIMALLDEECWFPKATDKSFVEKlAAAHSMHPKFMKTDfRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVV 646
Cdd:cd14886 423 FDKPNlSIFSFLEEQCLIQTGSSEKFTSS-CKSKIKNNSFIPGK-GSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDIL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 647 SLLQASQDPFVvqiwkdaeivgmaQQALTDTQFGARTRKGMFrtVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAG 726
Cdd:cd14886 501 ELLMGSTNPIV-------------NKAFSDIPNEDGNMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPN 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 727 KIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT--PNVIPKGFMDGKRACEQMIKSLELDSNLYRIGQS 804
Cdd:cd14886 566 KYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKT 645
|
....*
gi 158285519 805 KIFFR 809
Cdd:cd14886 646 KVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-766 |
1.70e-103 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 349.78 E-value: 1.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKgiKRHEVP------------PHVFAITDTAYRSM 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYA--YDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 168 LQDREDQSILCTGESGAGKTENTKKVIQYLAyvAASKPKGSVAVGVGCSLYFPWRSRNKhvqpcidcweasnslaeglsa 247
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFA--VHCGTGNNNLTNSESISPPASPSRTT--------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 248 lremrllwgkgeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DASGYISGANIETYLLEKSRAIRQAKDERT 326
Cdd:cd14899 136 ------------IEEQVLQSNPILEAFGNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 327 FHIFYQLLAG----ASPEQRERFILDDVKTYPFLSNGGLPVP---GVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAV 399
Cdd:cd14899 204 FHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLNQSLCSKrrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 400 LLFGSMTFKQ--ERNSDQATLPDNTVAQ----------KIAHLLGLNVTDMTKAfLTPR--------IKVGRDFVTKAQT 459
Cdd:cd14899 284 LHMGNVDFEQipHKGDDTVFADEARVMSsttgafdhftKAAELLGVSTEALDHA-LTKRwlhasnetLVVGVDVAHARNT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 460 REqvefaveAIAKACYEKMFKWLVNRINRSLDRT--------------KRQGASFIGILDMAGFEIFELNSFEQLCINYT 525
Cdd:cd14899 363 RN-------ALTMECYRLLFEWLVARVNNKLQRQasapwgadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYA 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 526 NEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKSFVEKLA---AAHS 601
Cdd:cd14899 436 NEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEhRPIGIFSLTDQECVFPQGTDRALVAKYYlefEKKN 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 602 MHPKFMKTD-FRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVVQIWKDAEIVGMAQQALTDTQFG 680
Cdd:cd14899 515 SHPHFRSAPlIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 681 ARTRKGMFRT----VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNR 756
Cdd:cd14899 595 RTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVR 674
|
730
....*....|
gi 158285519 757 IPFQEFRQRY 766
Cdd:cd14899 675 LTHKQFLGRY 684
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
98-808 |
6.57e-99 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 333.75 E-value: 6.57e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 98 LNEASVLHNIKDRYYSGLIYTY---SGLfcVVVNPYKKLPIYTEKIMEKYK-------GIKRHEVPPHVFAITDTAYRSM 167
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 168 LQDREDQSILCTGESGAGKTENTKKVIQYLAYVAASKPKGSVavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsa 247
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTK-------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 248 lremrllwgkgeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTF 327
Cdd:cd14879 121 ------------LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 328 HIFYQLLAGASPEQRERFILDDVKTYPFL-SNGGLPV---PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFG 403
Cdd:cd14879 189 HVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLplgPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 404 SMTFKQER-NSDQATLPDNT-VAQKIAHLLGLNVTDMTKAfLTPRIK-VGRDFVT----KAQTREQvefaVEAIAKACYE 476
Cdd:cd14879 269 NLEFTYDHeGGEESAVVKNTdVLDIVAAFLGVSPEDLETS-LTYKTKlVRKELCTvfldPEGAAAQ----RDELARTLYS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 477 KMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIF---ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwk 553
Cdd:cd14879 344 LLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVS-- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 554 fidfgLDLQPTID-------LIDKPGGIMALLDEEC-WFPKATDKSFVEKLAAAHSMHPKF----MKTDFRGVADFAVVH 621
Cdd:cd14879 422 -----VPATSYFDnsdcvrlLRGKPGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFiavgNFATRSGSASFTVNH 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 622 YAGKVDYSATKWLMKNMDPLNENVVSLLQASqdpfvvqiwkdaeivgmaqqaltdTQFgartrkgmfrtvshlyKEQLAK 701
Cdd:cd14879 497 YAGEVTYSVEGFLERNGDVLSPDFVNLLRGA------------------------TQL----------------NAALSE 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 702 LMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvipkgFMDG 781
Cdd:cd14879 537 LLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAA 610
|
730 740
....*....|....*....|....*..
gi 158285519 782 KRACEQMIKSLELDSNLYRIGQSKIFF 808
Cdd:cd14879 611 ERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-809 |
1.51e-89 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 307.13 E-value: 1.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKY---KGIKRHEVPPHVFAITDTAYRSMLQDREDQSIL 177
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 178 CTGESGAGKTENTKKVIQYLAYVAASKpkgsvavgvGCSLYfpwrSRNKHVqpcidcweasnslaeglsalremrllwgk 257
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSS---------RTTFD----SRFKHV----------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 258 geleqqllqaNPILEAFGNAKTVKNDNSSRFGKFIRINF-DASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG 336
Cdd:cd14878 119 ----------NCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 337 ASPEQRERFILDDVKTYPFLSNGglpVPGVDDYAE-------FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQ 409
Cdd:cd14878 189 LSAEEKYGLHLNNLCAHRYLNQT---MREDVSTAErslnrekLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 410 ERNSDQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRIN-- 487
Cdd:cd14878 266 LTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcc 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 488 -RSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID 566
Cdd:cd14878 346 lQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLD 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 567 -LIDKPGGIMALLDEECWFPKATDKSFVEKL----------AAAHSMHPKFMKTDFRGV-ADFAVVHYAGKVDYSATKWL 634
Cdd:cd14878 426 fFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqsllessntnAVYSPMKDGNGNVALKDQgTAFTVMHYAGRVMYEIVGAI 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 635 MKNMDPLNENVVsllqasqdpFVVQIWKDAEIVGMAQQALTdtqfgartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFV 714
Cdd:cd14878 506 EKNKDSLSQNLL---------FVMKTSENVVINHLFQSKLV--------------TIASQLRKSLADIIGKLQKCTPHFI 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 715 RCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVI-PKGFMDGKRACEQMIKSLE 793
Cdd:cd14878 563 HCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCK 642
|
730
....*....|....*.
gi 158285519 794 LDSnlYRIGQSKIFFR 809
Cdd:cd14878 643 LQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-809 |
1.73e-89 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 306.17 E-value: 1.73e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYtekiMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLayvaaskpkgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaegLSALREmrllwgKGEL 260
Cdd:cd14937 77 ESGSGKTEASKLVIKYY-----------------------------------------------LSGVKE------DNEI 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14937 104 SNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMtSEDFNSIFRIVSAVLLFGSMTFKQ-ER--NSDQAT 417
Cdd:cd14937 184 LKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQEiEKggKTNCSE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 418 LPDNT--VAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKr 495
Cdd:cd14937 263 LDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 496 QGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDlQPTIDLIDKPGGIM 575
Cdd:cd14937 342 ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSII 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 576 ALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDP 655
Cdd:cd14937 421 SILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNK 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 656 FVVQIWKDAEIvgmaqqalTDTQfgarTRKGMfrtVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLD 735
Cdd:cd14937 501 LVRSLYEDVEV--------SESL----GRKNL---ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFP 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 736 QLRCNGVLEGIRIcRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMIKSlELDSNLYRIGQSKIFFR 809
Cdd:cd14937 566 QLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
102-771 |
1.53e-88 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 301.43 E-value: 1.53e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKlpIYTEKIMEKYKGIKRHeVPPHVFAITDTAYRSMLQdREDQSILCTGE 181
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAyvaaskpkgsvavgvgcslyfpWRSRnkhvqpcidcweasnslaeglsalremrllwGKGELE 261
Cdd:cd14898 78 SGSGKTENAKLVIKYLV----------------------ERTA-------------------------------STTSIE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDasGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAgaspEQ 341
Cdd:cd14898 105 KLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCA----SK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RERFILDDVKTYPFLSNGGLPVPGVDDYaefQATVKSMNIMGMTSedFNSIFRIVSAVLLFGSMTFkqerNSDQAT-LPD 420
Cdd:cd14898 179 RLNIKNDFIDTSSTAGNKESIVQLSEKY---KMTCSAMKSLGIAN--FKSIEDCLLGILYLGSIQF----VNDGILkLQR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 421 NTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINRSLDRTkrqGASF 500
Cdd:cd14898 250 NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERS 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 501 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDE 580
Cdd:cd14898 327 ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISE 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 581 ECWFPKATDKSFVEKLaaaHSMHPKFMKTDFRGvaDFAVVHYAGKVDYSATKWLMKNMDPLNenvvsllqasqdpfvVQI 660
Cdd:cd14898 406 ESFNAWGNVKNLLVKI---KKYLNGFINTKARD--KIKVSHYAGDVEYDLRDFLDKNREKGQ---------------LLI 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 661 WKDAEIVgmaqqaltdtqfgartRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCN 740
Cdd:cd14898 466 FKNLLIN----------------DEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAEC 529
|
650 660 670
....*....|....*....|....*....|.
gi 158285519 741 GVLEGIRICRQGFPNRIPFQEFRQRYELLTP 771
Cdd:cd14898 530 GILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
101-809 |
2.77e-88 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 305.42 E-value: 2.77e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYS--------GLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDRE 172
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 173 DQSILCTGESGAGKTENTKKVIQYLAYVAASKpKGSVAVGvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremr 252
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRR-HGADSQG---------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 253 llwgkgeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQ 332
Cdd:cd14887 120 -------LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 333 LLAGAspeqrerfilddVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDfnsIFRIVSAVLLFGSMTFKQERN 412
Cdd:cd14887 193 LCNAA------------VAAATQKSSAGEGDPESTDLRRITAAMKTVGIGGGEQAD---IFKLLAAILHLGNVEFTTDQE 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 413 SDQATLPDNT--------VAQKIAHLL-------GLNVTDMTKAFLTPRIKVG------------RDFVTKAQTRE---- 461
Cdd:cd14887 258 PETSKKRKLTsvsvgceeTAADRSHSSevkclssGLKVTEASRKHLKTVARLLglppgvegeemlRLALVSRSVREtrsf 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 462 ----QVEFAVEAIAKACYEKMFKWLVNRINRSLDRTKR-------------QGASFIGILDMAGFEIFE---LNSFEQLC 521
Cdd:cd14887 338 fdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLC 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 522 INYTNEKLQQLFNHTMFILEQEEYQREG--IEWKFIDFGLDLQPTIDLIDKPGGIMALL------DEECWFPKATDKSFV 593
Cdd:cd14887 418 INYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPFSFPLASTLTSSPSSTSPFSptpsfrSSSAFATSPSLPSSL 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 594 EKLAAAHSMHPKFMKTDF---------------------------RGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVV 646
Cdd:cd14887 498 SSLSSSLSSSPPVWEGRDnsdlfyeklnkniinsakyknitpalsRENLEFTVSHFACDVTYDARDFCRANREATSDELE 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 647 SLLQASQDpfvvqiwkdaeivgMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAG 726
Cdd:cd14887 578 RLFLACST--------------YTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAG 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 727 KIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIpKGFMDGKRACEQMIKSLELDSNLYRIGQSKI 806
Cdd:cd14887 644 IFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKI 722
|
...
gi 158285519 807 FFR 809
Cdd:cd14887 723 FFR 725
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
102-789 |
3.98e-75 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 263.90 E-value: 3.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKK----LPIYTEKIMEKYkgikrhevpPHVFAITDTAYRSMLQDREDQSIL 177
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 178 CTGESGAGKTENTKKVIQYLAYVAASKPKGsvavgvgcslyfpwrsrnkhvqpcidcwEASNSLAEGLSALREMrllwgk 257
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAGGGPET----------------------------DAFKHLAAAFTVLRSL------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 258 geleqqllqanpileafGNAKTVKNDNSSRFGKFIRINFdASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGA 337
Cdd:cd14881 119 -----------------GSAKTATNSESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 338 SPEQRERFILD--DVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTsedFNSIFRIVSAVLLFGSMTFkQERNSDQ 415
Cdd:cd14881 181 SQEERVKLHLDgySPANLRYLSHGDTRQNEAEDAARFQAWKACLGILGIP---FLDVVRVLAAVLLLGNVQF-IDGGGLE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 416 ATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINrSLdrtKR 495
Cdd:cd14881 257 VDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SL---KR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 496 QGAS--------FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKF-IDFgLDLQPTID 566
Cdd:cd14881 333 LGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCID 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 567 LIDK-PGGIMALLDEECwFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENV 645
Cdd:cd14881 412 LISSlRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDL 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 646 VSLLQAsqdpfvvqiwkdaeivgmaqqalTDTQFGARTRKGMFRTvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRA 725
Cdd:cd14881 491 VAVFYK-----------------------QNCNFGFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETP 540
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 726 GKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKRACEQMI 789
Cdd:cd14881 541 NHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
101-761 |
4.41e-74 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 262.53 E-value: 4.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKGIKRHE-------VPPHVFAITDTAYRSMLQDRE 172
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 173 DQSILCTGESGAGKTENTKKVIQYLAYVAASKpkgsvavgvgcslyfpwrSRNkhvqpcidcweasnslaeglsalremr 252
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDS------------------QMT--------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 253 llwgkgELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA---------SGYISGANIETYLLEKSRAIRQAKD 323
Cdd:cd14884 116 ------ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 324 ERTFHIFYQLLAGASPEQ-RERFILDDVKTYPFLSN----------GGLPVPGVD----------DYAEFQATVKSMNIM 382
Cdd:cd14884 190 ERNFHVFYQVLRGLSDEDlARRNLVRNCGVYGLLNPdeshqkrsvkGTLRLGSDSldpseeekakDEKNFVALLHGLHYI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 383 GMTSEDFNSIFRIVSAVLLFGSMTFKQernsdqatlpdntvaqkIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQ 462
Cdd:cd14884 270 KYDERQINEFFDIIAGILHLGNRAYKA-----------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKEN 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 463 VEFAVEAIAKACYEKMFKWLVNRINRSLDRTKRQGA-----------SFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 531
Cdd:cd14884 333 ATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNN 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 532 LFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDKpggIMALLDE-----ECWFPKATDKSF-----------VEK 595
Cdd:cd14884 413 YYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK---IFRRLDDitklkNQGQKKTDDHFFryllnnerqqqLEG 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 596 LAAAHSMHPKfmktDFRGVAD--------FAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFvvqiwkdaeiv 667
Cdd:cd14884 489 KVSYGFVLNH----DADGTAKkqnikkniFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRF----------- 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 668 gmaqqaLTDTQFGArtRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIR 747
Cdd:cd14884 554 ------LREANNGG--NKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIK 625
|
730
....*....|....
gi 158285519 748 ICRQGFPNRIPFQE 761
Cdd:cd14884 626 ILNRGLSHKIPKKE 639
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
102-809 |
1.47e-72 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 257.71 E-value: 1.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMEKYKgiKRHEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAASKPKgsvavgvgcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkgEL 260
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSK----------------------------------------------------YL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14905 108 RDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDE 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGG-LPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNSDQatLP 419
Cdd:cd14905 188 EKAAYQLGDINSYHYLNQGGsISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTE--VK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 420 DNTVAQKIAHLLGLNVTDMTKAFLTPRikvgrdfvtKAQTREQVEfAVEAIAKACYEKMFKWLVNRINRSLDRTkrQGAS 499
Cdd:cd14905 266 DRTLIESLSHNITFDSTKLENILISDR---------SMPVNEAVE-NRDSLARSLYSALFHWIIDFLNSKLKPT--QYSH 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 500 FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKpggIMALLD 579
Cdd:cd14905 334 TLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLD 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 580 EECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRgvadFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVVQ 659
Cdd:cd14905 411 QESKNINSSDQIFLEKLQNFLSRHHLFGKKPNK----FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFS 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 660 iwKDAEIVGMAQQALTDTQFGAR--TRKGMFRTVSHLYK------------------------------------EQLAK 701
Cdd:cd14905 487 --RDGVFNINATVAELNQMFDAKntAKKSPLSIVKVLLScgsnnpnnvnnpnnnsgggggggnsgggsgsggstyTTYSS 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 702 LMDTLRNTNPN--FVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELltpnvipkgFM 779
Cdd:cd14905 565 TNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSF---------FF 635
|
730 740 750
....*....|....*....|....*....|....*...
gi 158285519 780 DGKRACEQMIKSLE-----LDSNL---YRIGQSKIFFR 809
Cdd:cd14905 636 QNQRNFQNLFEKLKendinIDSILpppIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-771 |
2.61e-72 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 255.57 E-value: 2.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 101 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYkgikrhevppHVFAITDTAYRSMLQDRED-QSILCT 179
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 180 GESGAGKTENTKKVIQYLAyvaaSKPKGSVAvgvgcslyfpwrsrNKHVqpcidcweasnslaeglSALREmrllwgkge 259
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT----SQPKSKVT--------------TKHS-----------------SAIES--------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 260 leqqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDASgYISGANIE-TYLLEKSRAIRQAKDERTFHIFYQLLAGAS 338
Cdd:cd14874 107 ----------VFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLN 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 339 PEQRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTFKQERNS----D 414
Cdd:cd14874 176 DEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPnveqD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 415 QATLPDNTVAQKIAHLLGLNVtDMTKAFLTPRIKVGRDFVTKAQTREQvefavEAIAKACYEKMFKWLVNRINRSLDRTK 494
Cdd:cd14874 256 VVEIGNMSEVKWVAFLLEVDF-DQLVNFLLPKSEDGTTIDLNAALDNR-----DSFAMLIYEELFKWVLNRIGLHLKCPL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 495 RQGAsfIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDF----GLDLQPTIDLI-D 569
Cdd:cd14874 330 HTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfK 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 570 KPGGIMALLDEECWFPKATDKSFVEKLAAAHSMHPKFMKTDFRGVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLL 649
Cdd:cd14874 405 KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLL 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 650 QASQDPFVVQIWKDA------EIVGMAQQALTDTQfgartrkgmfrtvshlykeqlaKLMDTLRNTNPNFVRCIIPNHEK 723
Cdd:cd14874 485 RSSKNPIIGLLFESYssntsdMIVSQAQFILRGAQ----------------------EIADKINGSHAHFVRCIKSNNER 542
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 158285519 724 RAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 771
Cdd:cd14874 543 QPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLP 590
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-809 |
8.96e-67 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 239.64 E-value: 8.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGE 181
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 182 SGAGKTENTKKVIQYLAYVAASKPkgsvavGVGcslyfpwrsrnkhvqpcidcweasnslaeglsalremrllwgkgele 261
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNR------GAT----------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 262 QQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPEQ 341
Cdd:cd14882 109 GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQN 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 342 RER-FILDDVKTYPFL----SNGGL--------PVPGVDDYAEFQATVKSMNimgMTSEDFNSIFRIVSAVLLFGSMTFK 408
Cdd:cd14882 189 RLKeYNLKAGRNYRYLrippEVPPSklkyrrddPEGNVERYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRFR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 409 QerNSDQATLPDNTVAQKIAHLLGLNVTDMTKAFLTPRIKVGRDFVTKAQTREQVEFAVEAIAKACYEKMFKWLVNRINR 488
Cdd:cd14882 266 Q--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINM 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 489 SLDRTKrqgASF-----IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQP 563
Cdd:cd14882 344 KMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKT 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 564 TID-LIDKPGGIMALLDEECwfPKATDKSFVekLAAAHSMHPKFMKTDfrGVADFAVVHYAGKVDYSATKWLMKNMDPLN 642
Cdd:cd14882 420 AVDqLMTKPDGLFYIIDDAS--RSCQDQNYI--MDRIKEKHSQFVKKH--SAHEFSVAHYTGRIIYDAREFADKNRDFVP 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 643 ENVVSLLQASQDPFVVQIWKDAEIVGMaqqaltdtqfgaRTRKGMFRTVShlyKEQLAKLMDTLRNTNPNFVRCIIPNHE 722
Cdd:cd14882 494 PEMIETMRSSLDESVKLMFTNSQVRNM------------RTLAATFRATS---LELLKMLSIGANSGGTHFVRCIRSDLE 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 723 KRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDgKRACEQMIKSLELDSnlYRIG 802
Cdd:cd14882 559 YKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIG 635
|
....*..
gi 158285519 803 QSKIFFR 809
Cdd:cd14882 636 KTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
104-808 |
2.55e-64 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 234.87 E-value: 2.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 104 LHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKR----------HEVPPHVFAITDTAYRSMLQDRED 173
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 174 QSILCTGESGAGKTENTKKVIQYLAYVAASkpkgsvavgvgcslyfpwrsrnkhVQPCIDCWEASNSLAEglsalremrl 253
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDE------------------------TEPRPDSEGASGVLHP---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 254 lwgkgeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGYISGANIETYLLEKSRAIRQAKDERTFHIFYQL 333
Cdd:cd14893 130 ------IGQQILHAFTILEAFGNAATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 334 LAGAS--PEQRERFILDD-VKTYPFLSNGGLPVPGVD-DYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMTF-- 407
Cdd:cd14893 204 LAGVQhdPTLRDSLEMNKcVNEFVMLKQADPLATNFAlDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvp 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 408 -----KQERNSDQATLPD-NTVAQK-------IAHLLGLNVTDMTKAFLTPRI--KVGRDFVT--KAQTREQVEFAVEAI 470
Cdd:cd14893 284 dpeggKSVGGANSTTVSDaQSCALKdpaqillAAKLLEVEPVVLDNYFRTRQFfsKDGNKTVSslKVVTVHQARKARDTF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 471 AKACYEKMFKWLVNRINRSL----DRTKRQG----ASFIGILDMAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI 539
Cdd:cd14893 364 VRSLYESLFNFLVETLNGILggifDRYEKSNivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 540 ----LEQEEYQREG--IEWKFIDFGLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKSFVEKLAAAH---------SMH 603
Cdd:cd14893 444 nfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFeDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavgglsrpNMG 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 604 PKFMKTDFRGVAD----FAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQDPFVvqiwkdaEIVGMAQQALTDTQF 679
Cdd:cd14893 524 ADTTNEYLAPSKDwrllFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVL-------HAVGAAQMAAASSEK 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 680 GA------RTRKGMFRTVSHLYKE--------------QLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRC 739
Cdd:cd14893 597 AAkqteerGSTSSKFRKSASSAREsknitdsaatdvynQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRM 676
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 740 NGVLEGIRICRQGFPNRIPFQEFRQRYElltpNVIpkgfmdGKRAC-EQMIKSLE----LDSNLYRIGQSKIFF 808
Cdd:cd14893 677 NHLVELMQASRSIFTVHLTYGHFFRRYK----NVC------GHRGTlESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-807 |
7.51e-58 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 214.70 E-value: 7.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 102 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMEKYKGIKR-HEVPPHVFAITDTAYRSMLQDREDQSILCTG 180
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCiEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 181 ESGAGKTENTKKVIQYLAYVAaskpKGSVAVGVGCSLYFPWRSRNKHVQPcidcweasnslaeglsalremrllwGKGEL 260
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQV----KGSRRLPTNLNDQEEDNIHNEENTD-------------------------YQFNM 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 261 EQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASgYISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGASPE 340
Cdd:cd14938 133 SEMLKHVNVVMEAFGNAKTVKNNNSSRFSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 341 QRERFILDDVKTYPFLSNGGLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFG----------------- 403
Cdd:cd14938 212 FKKMYFLKNIENYSMLNNEKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGnteivkafrkksllmgk 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 404 ---SMTFKQE------RNSDQATLPDNTVAQKIA-HLLGLNVTDMTKAFLTPRIkVGRDFVTKAQTREQVEFAVEAIAKA 473
Cdd:cd14938 292 nqcGQNINYEtilselENSEDIGLDENVKNLLLAcKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 474 CYEKMFKWLVNRINRSLDRTKR--QGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE 551
Cdd:cd14938 371 CYEELFNWIIYKINEKCTQLQNinINTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIF 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 552 WKFIDFGLDLQPTIDLIDKP--GGIMALLDEECwFPKATDKSFVEKLAAAHSMH-PKFMKTD--FRGVADFAVVHYAGKV 626
Cdd:cd14938 451 CEYNSENIDNEPLYNLLVGPteGSLFSLLENVS-TKTIFDKSNLHSSIIRKFSRnSKYIKKDdiTGNKKTFVITHSCGDI 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 627 DYSATKWLMKNMDPLNENVVSLLQASQDPFVVQIW------KDAEIVG-----MAQQALTDTQFGARTRKGMFRTvshLY 695
Cdd:cd14938 530 IYNAENFVEKNIDILTNRFIDMVKQSENEYMRQFCmfynydNSGNIVEekrrySIQSALKLFKRRYDTKNQMAVS---LL 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 696 KEQLAKLMDTLRNTNPNFVRCIIPNHEKRA-GKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvi 774
Cdd:cd14938 607 RNNLTELEKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--- 683
|
730 740 750
....*....|....*....|....*....|...
gi 158285519 775 pkgfmDGKRACEQMIKSLELDSNLYRIGQSKIF 807
Cdd:cd14938 684 -----DLKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
123-301 |
3.05e-52 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 181.39 E-value: 3.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 123 FCVVVNPYKKLPIYTE-KIMEKYKGIKRHEVPPHVFAITDTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAYVA 201
Cdd:cd01363 1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 202 AS-KPKGSVAVGVGCSlyfpwrsrnkhvqpcidcweasnslaeglsalremrllWGKGELEQQLLQANPILEAFGNAKTV 280
Cdd:cd01363 81 FNgINKGETEGWVYLT--------------------------------------EITVTLEDQILQANPILEAFGNAKTT 122
|
170 180
....*....|....*....|.
gi 158285519 281 KNDNSSRFGKFIRINFDASGY 301
Cdd:cd01363 123 RNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
884-1650 |
8.59e-33 |
|
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: 139.42 E-value: 8.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKL---VQKEDELRQIRDKLENLSKNS-----QEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARK 955
Cdd:TIGR02168 197 ELERQLKSLerqAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 956 QELEELMQDLESRIEEEEERVNALTSEKKK-------LQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALI 1028
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQIlrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1029 EDQNHKLVKEKKLLEERANDLsQTLAEEEEKAKHLAKLKV-KHESTIAELEERL--LKDHQQRQEADRS---KRKIETEV 1102
Cdd:TIGR02168 357 EAELEELEAELEELESRLEEL-EEQLETLRSKVAQLELQIaSLNNEIERLEARLerLEDRRERLQQEIEellKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1103 ADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIqEDLEAEKLARSKAEKQKRDL 1182
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1183 NEELEALKNELLDSLDTTA------------AQQELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQL 1250
Cdd:TIGR02168 515 QSGLSGILGVLSELISVDEgyeaaieaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1251 ENLKKMKG---GLEKSKQQLE------------AENADLATELRN----------------------------VNQSRQE 1287
Cdd:TIGR02168 595 KNIEGFLGvakDLVKFDPKLRkalsyllggvlvVDDLDNALELAKklrpgyrivtldgdlvrpggvitggsakTNSSILE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1288 NDR-------RRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQ 1360
Cdd:TIGR02168 675 RRReieeleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1361 LLEEETRQKLALSSKLRQIESEKEALqeqleedeeaktnyEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDI- 1439
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEA--------------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAa 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1440 ------ETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAE 1513
Cdd:TIGR02168 821 nlrerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1514 REAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELAN--------TQGTADKNVHELEKAKRALESQLAELKAQ 1585
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseeyslTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 1586 NEELEddlqltedaklrlEVNMQALrAQFERDIQAKEEQSEEKrRGLVKALRDLE---AELDEERKQR 1650
Cdd:TIGR02168 981 IKELG-------------PVNLAAI-EEYEELKERYDFLTAQK-EDLTEAKETLEeaiEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1017-1650 |
1.42e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.98 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1017 KLKKMEEDVALIEDQNHKLVKEKKLLEERANDLS--QTLAEEEEKAKHLAKLKV--KHESTIAELEERLLKDHQQRQEAD 1092
Cdd:COG1196 180 KLEATEENLERLEDILGELERQLEPLERQAEKAEryRELKEELKELEAELLLLKlrELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1093 RSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLAR 1172
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1173 SKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDEsanhestlmdmrhkhAQEISSINEQLEN 1252
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA---------------LRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1253 LKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQ 1332
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1333 QLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQ 1412
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1413 EMKKRSE---EDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQK 1489
Cdd:COG1196 565 YLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1490 NFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELE 1569
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1570 KAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALR---AQFERDIQAK-----------EEQSE------EKR 1629
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELErelERLEREIEALgpvnllaieeyEELEErydflsEQR 804
|
650 660
....*....|....*....|....
gi 158285519 1630 RGLVKALRDLE---AELDEERKQR 1650
Cdd:COG1196 805 EDLEEARETLEeaiEEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1757 |
6.39e-30 |
|
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: 130.18 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 978 ALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQ-----LDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQT 1052
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREELEELQEELKEAEeeleeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1053 LAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEAdrskrkiETEVADLKEQINERRMQIEEMQQQLVKREEELAq 1132
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-------AEELAELEEKLEELKEELESLEAELEELEAELE- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1133 tlvrideesaakaaaqktqrELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSldttaaqQELRSKREQ 1212
Cdd:TIGR02168 369 --------------------ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-------EDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1213 EVATLKKTLEDESanhestlmdmRHKHAQEISSINEQLEnlkkmkgglekskqQLEAENADLATELRNVNQSRQENDRRR 1292
Cdd:TIGR02168 422 EIEELLKKLEEAE----------LKELQAELEELEEELE--------------ELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1293 KQAETQIAELQVKLAdvdrvrvELQDKVTKLQQESENITQQLDEAELKAS--AAIKSAGNLESQLTEAQQLLEEETRQKL 1370
Cdd:TIGR02168 478 DAAERELAQLQARLD-------SLERLQENLEGFSEGVKALLKNQSGLSGilGVLSELISVDEGYEAAIEAALGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1371 A---LSSKLRQIESEKEALQEQLEEDEEAKTNYekklAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQI- 1446
Cdd:TIGR02168 551 VvenLNAAKKAIAFLKQNELGRVTFLPLDSIKG----TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVl 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1447 --QELQAANDRLdkskKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAIsEQVAQERDAAEREAREKETKVL 1524
Cdd:TIGR02168 627 vvDDLDNALELA----KKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1525 SLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLE 1604
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1605 VNMQALRAQFERDIQAKEEQSEekrrglvkALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQ 1684
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALRE--------ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158285519 1685 AKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINS 1757
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1017-1892 |
1.35e-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: 129.02 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1017 KLKKMEEDVALIEDQNHKLVKEKKLLE---ERANDLSQTLAEEEEKAKHLAKLKVKhestiaELEERLLKDHQQRQEADR 1093
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLErqaEKAERYKELKAELRELELALLVLRLE------ELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1094 SKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARS 1173
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1174 KAEKQKRDLNEELEALKNELldsldttAAQQELRSKREQEVATLKKTLEDESANHEsTLMDMRHKHAQEISSINEQLENL 1253
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESRLEELEEQLE-TLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1254 KKMKGGLEKSKQQLEAENADLATELrnVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQ 1333
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1334 LDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKE--------------------ALQEQLEED 1393
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalggrlqavvvenLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1394 EEAKTNYEK---------KLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQI---QELQAANDRLdkskK 1461
Cdd:TIGR02168 564 FLKQNELGRvtflpldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELA----K 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1462 KIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAIsEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELE 1541
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1542 TKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAK 1621
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1622 EEQSEekrrglvkALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAirdaee 1701
Cdd:TIGR02168 799 KALRE--------ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL------ 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1702 akaakeelaaiskesERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSnsskgslmiDEKRRLEARiaaleE 1781
Cdd:TIGR02168 865 ---------------EELIEELESELEALLNERASLEEALALLRSELEELSEELRE---------LESKRSELR-----R 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1782 ELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKS-NSQNNETLKCGLERLNKELKAKLSEqetaLRTKLKA-----ATA 1855
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKR----LENKIKElgpvnLAA 991
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 158285519 1856 ASEAKNLN-----LEKQLENETKERLAVQKANRKLEKRIKEL 1892
Cdd:TIGR02168 992 IEEYEELKerydfLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1289-1933 |
3.49e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1289 DRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESEN----ITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEE 1364
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1365 ETRQKLALSSKLRQIESEKEALqeqleedeeaktnyEKKLAELNFTIQEMKKRSEEdsdiakeLEESKKKMNKDIETLQR 1444
Cdd:COG1196 251 LEAELEELEAELAELEAELEEL--------------RLELEELELELEEAQAEEYE-------LLAELARLEQDIARLEE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1445 QIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKqknfdkvLAEEKAISEQVAQERDAAEREAREKETKVL 1524
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE-------LEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1525 SLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLE 1604
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1605 VNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQ 1684
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1685 AkkLQAQIKDAIRDAEEAKAAKEELAAISKESerKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSnsskgsl 1764
Cdd:COG1196 543 A--LAAALQNIVVEDDEVAAAAIEYLKAAKAG--RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA------- 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1765 miDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQET 1844
Cdd:COG1196 612 --DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1845 ALRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNL 1924
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
....*....
gi 158285519 1925 DEAEEEIQK 1933
Cdd:COG1196 770 ERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
952-1554 |
5.57e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.51 E-value: 5.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 952 VARK-QELEELMQDLE-----SRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDV 1025
Cdd:COG1196 211 KAERyRELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1026 ALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADL 1105
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1106 KEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEE 1185
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1186 LEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHEStLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQ 1265
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL-LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1266 QLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAI 1345
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1346 KsagnLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIA 1425
Cdd:COG1196 610 E----ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1426 KELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQV 1505
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 158285519 1506 AQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDEL 1554
Cdd:COG1196 766 ERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETL 814
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
107-750 |
6.67e-28 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 122.93 E-value: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 107 IKDRYYSGLIYTYSGLFCV-VVNPYKKL------PIYTEKIMEKYKGIKRHE--VPPHVFAI------------------ 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 160 --TDTAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAYVAasKPKGSVAVGVGCSLYFPWRsrnkhvQPCIDCWEA 237
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVA--QPALSKGSEETCKVSGSTR------QPKIKLFTS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 238 S--NSLAEGLSALREMRLLWGKG-----------------------------------------------ELEQQL---- 264
Cdd:cd14894 158 StkSTIQMRTEEARTIALLEAKGvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehlEDEEQLrmyf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 265 ------------LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDASGY---ISGANIETYLLEKSRAIRQA------ 321
Cdd:cd14894 238 knphaakklsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgd 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 322 KDERTFHIFYQLLAG--ASPEQR---ERFILD--DVKTYPFLSNGGLPVPGV--------DDYAEFQATVKSMNIMGMTS 386
Cdd:cd14894 318 QNELNFHILYAMVAGvnAFPFMRllaKELHLDgiDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 387 EDFNSIFRIVSAVLLFGSMTFKQERNSDQATLPDN---TVAQKIAHLLGL-NVTDMTKAFLTPRIKVGRDFVTKAQTRE- 461
Cdd:cd14894 398 DEQKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEk 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 462 -QVEFAVEAIAKACYEKMFKWLVNRINR-------SLDRTKRQ---------GASFIGILDMAGFEIFELNSFEQLCINY 524
Cdd:cd14894 478 gQVNHVRDTLARLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINY 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 525 TNEKLqqlfnhtmfileqeeYQREGiewKFIDFGLDLQP----------TIDLIDKPGGIMALLDEECWFPKAT------ 588
Cdd:cd14894 558 LSEKL---------------YAREE---QVIAVAYSSRPhltardsekdVLFIYEHPLGVFASLEELTILHQSEnmnaqq 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 589 ----DKSFVEKLAAAHSMH----PKFMKTDFR------GVADFAVVHYAGKVDYSATKWLMKNMDPLNENVVSLLQASQD 654
Cdd:cd14894 620 eekrNKLFVRNIYDRNSSRlpepPRVLSNAKRhtpvllNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNS 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 655 PFVVQIWKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVL 734
Cdd:cd14894 700 SHFCRMLNESSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVE 779
|
810
....*....|....*.
gi 158285519 735 DQLRCNGVLEGIRICR 750
Cdd:cd14894 780 QQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1243-1966 |
8.11e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 123.24 E-value: 8.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1243 ISSINEQLENLKKMKGGLEKSKQQLEAENA-----------DLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDR 1311
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRElelallvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1312 VRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLE 1391
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1392 EDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDAT 1471
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1472 IELDTQR--TKVLELEKKQKNFDKVLAEEKAISEQVA---QERDAAEREAREKETKVLSLTReLDEAFEKIDELEtkrKG 1546
Cdd:TIGR02168 435 LKELQAEleELEEELEELQEELERLEEALEELREELEeaeQALDAAERELAQLQARLDSLER-LQENLEGFSEGV---KA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1547 LQNELDELANTQGTADKNVHELEKAKRALESQLAELkAQNEELEDDlqltEDAKLRLE---------VNMQALRAQFERD 1617
Cdd:TIGR02168 511 LLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGR-LQAVVVENL----NAAKKAIAflkqnelgrVTFLPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1618 IQAKEEQSEEKRRGLVKALRDLEaeldeerkqraaavAAKKKLEGDLKDMEATLEMNNKVkEDALKQAKKLQAQIKDAIR 1697
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLV--------------KFDPKLRKALSYLLGGVLVVDDL-DNALELAKKLRPGYRIVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1698 D-------------AEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSL 1764
Cdd:TIGR02168 651 DgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1765 MIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQET 1844
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1845 AL-RTKLKAATAASEAKNLNLEKQLENETKERLAVQKANR-----KLEKRIKELTMNIEDERRHADQYKEQIEKANNRMK 1918
Cdd:TIGR02168 811 ELtLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsedieSLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 158285519 1919 TLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKL 1966
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1154-1955 |
3.83e-27 |
|
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: 120.93 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1154 LESQLAEIQEDLEAEKLARSKAEKQKrDLNEELEALKNELLdSLDTTAAQQELRSKREQEvatlkktledESANHEstlm 1233
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELEELQEEL----------KEAEEE---- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1234 dmRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVR 1313
Cdd:TIGR02168 255 --LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1314 VELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEalqeqleed 1393
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE--------- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1394 eeaktNYEKKLAELNftiQEMKKRSEEDSDIAKELEESKKKMNK-DIETLQRQIQELQAANDRLDKSKKKIQSELEDATI 1472
Cdd:TIGR02168 404 -----RLEARLERLE---DRRERLQQEIEELLKKLEEAELKELQaELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1473 ELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAER------------EAREKETKVLS----------LTREL 1530
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEaalggrlqavVVENL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1531 DEAFEKIDELETKRKG--------------LQNELDELANTQ----GTADKNVHELEKAKRALESQLAE----------L 1582
Cdd:TIGR02168 556 NAAKKAIAFLKQNELGrvtflpldsikgteIQGNDREILKNIegflGVAKDLVKFDPKLRKALSYLLGGvlvvddldnaL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1583 KAQNEELEDDLQLTEDAKL----------RLEVNMQAL-RAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRA 1651
Cdd:TIGR02168 636 ELAKKLRPGYRIVTLDGDLvrpggvitggSAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1652 AAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLT 1731
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1732 EDLSSSERARRAAEGERDELLEEINSNSSKgslmideKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTEL 1811
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRER-------LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1812 ATEKSNSQNNETLKCGLERLNKELKAKLSEQETALRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKE 1891
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1892 LTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDE-------AEEEIQKEKTLKRKAQRECEDMLESHEAL 1955
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
882-1649 |
1.45e-26 |
|
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: 119.02 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 882 LLEVTKQEEKLVQKEDELRQIRDKLEN----------LSKNSQEYE-----KKYQQAMEEKTHLAEQL---QAEIE-LCA 942
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRRerekaeryqaLLKEKREYEgyellKEKEALERQKEAIERQLaslEEELEkLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 943 EAEEGRARLVARKQELEEL----MQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKL 1018
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1019 KKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAK----HLAKLKVKHESTIAELEE-----RLLKDHQQRQ 1089
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdELKDYREKLEKLKREINElkrelDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1090 EADRskRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDL---E 1166
Cdd:TIGR02169 419 SEEL--ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1167 AEKLARSKAEKQKRDLNEELEA------------------------------LKNELLDSLDTTAAQQELRSKREQEVAT 1216
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKAsiqgvhgtvaqlgsvgeryataievaagnrLNNVVVEDDAVAKEAIELLKRRKAGRAT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1217 ------LKKTLEDESANHESTLMDmrhkHAQEISSINEQLENLKKMKGG-------LEKSKQQL-EAENADLATELRNVN 1282
Cdd:TIGR02169 577 flplnkMRDERRDLSILSEDGVIG----FAVDLVEFDPKYEPAFKYVFGdtlvvedIEAARRLMgKYRMVTLEGELFEKS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1283 QSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLL 1362
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1363 EEETRQKLALSSKLRQIESEKEALQEQleedeeaKTNYEKKLAELNFTIQEMKkrsEEDSDIAKELEESKkkmnkdIETL 1442
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSE-------LKELEARIEELEEDLHKLE---EALNDLEARLSHSR------IPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1443 QRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETK 1522
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1523 VLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLT---EDA 1599
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDV 956
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 158285519 1600 KLRLEVNMQALRAQFERDIQAKEEQSEEKRRglVKALRDLEAELDEERKQ 1649
Cdd:TIGR02169 957 QAELQRVEEEIRALEPVNMLAIQEYEEVLKR--LDELKEKRAKLEEERKA 1004
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1013-1847 |
3.01e-25 |
|
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: 114.78 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1013 QLDAKLKKMEEDVALIEDQnhklVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKvkhestiAELEERLLKDH-QQRQEA 1091
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEEN----IERLDLIIDEKRQQLERLRREREKAERYQALL-------KEKREYEGYELlKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1092 DRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQ-RELESQLAEIQEDLEAEKL 1170
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1171 ARSKAEKQKRDLNEELEALKNELlDSLDTtaAQQELRSKREQevatlkktLEDESANHESTLMDMRHKHAQEISSINEQL 1250
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEI-EELER--EIEEERKRRDK--------LTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1251 ENLKKMKGGLEKSKQQLEaenaDLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENI 1330
Cdd:TIGR02169 385 DELKDYREKLEKLKREIN----ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1331 TQQLDEAELKASaaiksagnlesQLTEAQQLLEEETRQklaLSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFT 1410
Cdd:TIGR02169 461 AADLSKYEQELY-----------DLKEEYDRVEKELSK---LQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1411 IQEMKKRSE-------------------EDSDIAKELEESKKKMN------------KDIETLQRQIQE---LQAANDRL 1456
Cdd:TIGR02169 527 VAQLGSVGEryataievaagnrlnnvvvEDDAVAKEAIELLKRRKagratflplnkmRDERRDLSILSEdgvIGFAVDLV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1457 DKSKKK------------IQSELEDATIELDTQRTKVLELEkkqknfdkVLAEEKAISEQVAQERDAAEREAREKEtKVL 1524
Cdd:TIGR02169 607 EFDPKYepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEGE--------LFEKSGAMTGGSRAPRGGILFSRSEPA-ELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1525 SLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLE 1604
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1605 VNMQALRA---QFERDIQAKEEQSEE-KRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKED 1680
Cdd:TIGR02169 758 SELKELEArieELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1681 ALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSS 1760
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1761 KGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRnRKAQLTIEQLTTEL-ATEKSNSQNNETLKCGLERLN--KELKA 1837
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLDelKEKRA 996
|
890
....*....|
gi 158285519 1838 KLSEQETALR 1847
Cdd:TIGR02169 997 KLEEERKAIL 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1152-1730 |
2.24e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1152 RELESQLaeiqEDLEAEklaRSKAEKqKRDLNEELEALKNEL-LDSLDTTAAQQELRSKREQEVATLKKTLEDESANHES 1230
Cdd:COG1196 196 GELERQL----EPLERQ---AEKAER-YRELKEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1231 TLMDMRHKHAQEISSINEQLENLKKmkggLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVD 1310
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYE----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1311 RVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQL 1390
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1391 EEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDA 1470
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1471 tiELDTQRTKVLELEKKQKNFDKVLAEEkaISEQVAQERDAAEREAREKETKVlslTRELDEAFEKIDELETKRKGLQNE 1550
Cdd:COG1196 504 --EGFLEGVKAALLLAGLRGLAGAVAVL--IGVEAAYEAALEAALAAALQNIV---VEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1551 LDELANTQGTADKNVHE---LEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDI--------- 1618
Cdd:COG1196 577 LPLDKIRARAALAAALArgaIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRevtlegegg 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1619 -----------QAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKK 1687
Cdd:COG1196 657 saggsltggsrRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 158285519 1688 LQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQL 1730
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
882-1494 |
6.89e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.41 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 882 LLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEEL 961
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 962 MQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKL 1041
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1042 LEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQ 1121
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1122 QLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLAR---------SKAEKQKRDLNEELEALKNE 1192
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavliGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1193 LLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSIneqlenlkkmkgglekskQQLEAENA 1272
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV------------------ASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1273 DLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLE 1352
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1353 SQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDsdiAKELEESK 1432
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD---LEELEREL 769
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1433 KKMNKDIETL----QRQIQELQAANDRLDKSKKKIQ------SELEDATIELDTQRTKVLelekkQKNFDKV 1494
Cdd:COG1196 770 ERLEREIEALgpvnLLAIEEYEELEERYDFLSEQREdleearETLEEAIEEIDRETRERF-----LETFDAV 836
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1243-1955 |
1.83e-22 |
|
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: 105.92 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1243 ISSINEQLENLKKMKGGLEKSKqqleaenaDLATELRNVNQ-----SRQENDRRRKQAETQIAELQVKLADVDRVRVELQ 1317
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQ--------ALLKEKREYEGyellkEKEALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1318 DKVTKLQQESENITQQLDEAELKASAAIKSA--------GNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQ 1389
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1390 LEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELED 1469
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1470 ATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQN 1549
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1550 ELDELANTQGTADKN-------VHELEKAKR----ALESQlAELKAQNEELEDDlqltEDAKLRLEV--NMQALRAQF-- 1614
Cdd:TIGR02169 505 RVRGGRAVEEVLKASiqgvhgtVAQLGSVGEryatAIEVA-AGNRLNNVVVEDD----AVAKEAIELlkRRKAGRATFlp 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1615 -------ERDIQAKEEQS-----------EEKRRGLVK-ALRDLEAELDEERKQRAAAVAAKKKLEGDL----------- 1664
Cdd:TIGR02169 580 lnkmrdeRRDLSILSEDGvigfavdlvefDPKYEPAFKyVFGDTLVVEDIEAARRLMGKYRMVTLEGELfeksgamtggs 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1665 -----------KDMEATLEMNNKVKE---------DALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLE 1724
Cdd:TIGR02169 660 raprggilfsrSEPAELQRLRERLEGlkrelsslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1725 ADLMqltEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALE-EELEEEQSNLELMVDRNRKAQLT 1803
Cdd:TIGR02169 740 EELE---EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1804 IEQ----LTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQETALRtKLKAATAASEAKNLNLEKQLENETKERLAVQ 1879
Cdd:TIGR02169 817 IEQklnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELE 895
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1880 KANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLkRKAQRECEDMLESHEAL 1955
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRAL 970
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
874-1697 |
3.55e-21 |
|
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: 101.59 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 874 RLYTKVKPLLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKyqQAMEEKTHLAEQLQAEIELCAEAEEGRARLVA 953
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL--KEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 954 RKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEA-ARQKLQLEKVQLDAKLKKMEEDVALIEDQN 1032
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEeLKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1033 HKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINER 1112
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1113 RMQIEEMQQQLVKREEELAQTLVRIDEEsaakAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNE 1192
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEE----EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1193 LLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLE----------- 1261
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEvsatadeveer 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1262 KSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKL------ADVDRVRVELQDKVTKLQQESENITQQLD 1335
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLdkatleADEDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1336 EAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMK 1415
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1416 --KRSEEDSDIAKELEESKKKMNKDIETLQRQIQE-LQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFD 1492
Cdd:pfam02463 724 adRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1493 KVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAK 1572
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1573 RALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAA 1652
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 158285519 1653 AVAAKKKLEGDLKDMEATLEMNNKVKEDALK-QAKKLQAQIKDAIR 1697
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDElEKERLEEEKKKLIR 1009
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
886-1554 |
1.55e-20 |
|
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: 98.94 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 886 TKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLqaeielcaeaeegrarlvarkQELEELMQDL 965
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKI---------------------KILEQQIKDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 966 ESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDV----ALIEDQNHKLVKEKKL 1041
Cdd:TIGR04523 88 NDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIkkkeKELEKLNNKYNDLKKQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1042 LEERANDLSQTLAEEEEKAKHLAklKVKHESTIAELEERLLKDHQQRQeadrskRKIETEVADLKEQINERRMQIEEMQQ 1121
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNID--KIKNKLLKLELLLSNLKKKIQKN------KSLESQISELKKQNNQLKDNIEKKQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1122 QLVKREEELAQTlvrideesaakaaaQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDsldtta 1201
Cdd:TIGR04523 240 EINEKTTEISNT--------------QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1202 aqqeLRSKREQEvatLKKTLEDESANHESTLMDMRH---KHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATEL 1278
Cdd:TIGR04523 300 ----LNNQKEQD---WNKELKSELKNQEKKLEEIQNqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1279 RNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEA 1358
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1359 QQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKD 1438
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1439 IETLQRQIQELQAANDRLDKSKKKIQSEledatIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREARE 1518
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELKKENLE-----KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
650 660 670
....*....|....*....|....*....|....*.
gi 158285519 1519 KETKVLSLTRELDEAFEKIDELETKRKGLQNELDEL 1554
Cdd:TIGR04523 608 KEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
951-1576 |
1.81e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 98.98 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 951 LVARKQELEELMQDLESRIEEEEERVNALTSEKKKLqiniqdleeqleeeEAARQKLQLEKvqldAKLKKMEEDVALIED 1030
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPEL--------------REELEKLEKEV----KELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1031 QNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKlKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQIN 1110
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1111 ERRMQIEEMqQQLVKREEELaqtlvrideesaakaaaQKTQRELESQLAEIQEDLEAEKLARSKAEK----QKRDLNEEL 1186
Cdd:PRK03918 325 GIEERIKEL-EEKEERLEEL-----------------KKKLKELEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1187 EALKNELldsldttaaqqelrskreQEVATLKKTLEDEsanhESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQ 1266
Cdd:PRK03918 387 EKLEKEL------------------EELEKAKEEIEEE----ISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1267 LEAEN-----ADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELqdKVTKLQQESENITQQLDEAELKA 1341
Cdd:PRK03918 445 LTEEHrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELAEQLKELEEKLKKYNLEELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1342 SAaiksagnlesqlTEAQQLLEEETRQKLALSSKLRQIESEKEalqeqleedeeaktnYEKKLAELNFTIQEMKkrsEED 1421
Cdd:PRK03918 523 KA------------EEYEKLKEKLIKLKGEIKSLKKELEKLEE---------------LKKKLAELEKKLDELE---EEL 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1422 SDIAKELEEskkKMNKDIETLQRQIQELQAANDRLdKSKKKIQSELEDATIELDTQRTkvlELEKKQKNFDKVLAEEKAI 1501
Cdd:PRK03918 573 AELLKELEE---LGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEE---ELDKAFEELAETEKRLEEL 645
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1502 SEQVAQ-ERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALE 1576
Cdd:PRK03918 646 RKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
895-1649 |
2.38e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 895 KEDELRQIRDKLENlsKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQEleELMQDLESRIEEEEE 974
Cdd:PTZ00121 1077 KDFDFDAKEDNRAD--EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE--DARKAEEARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 975 RVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLA 1054
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1055 EEEEKAKHLAKL--KVKHESTIAELEERLLKDHQQRQEADRSKrkiETEVADLKEQINERRMQIEEMQQQLVKREEELAQ 1132
Cdd:PTZ00121 1233 EEAKKDAEEAKKaeEERNNEEIRKFEEARMAHFARRQAAIKAE---EARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1133 TLvridEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNElldsldTTAAQQELRSKREQ 1212
Cdd:PTZ00121 1310 KA----EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK------AEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1213 EVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENAdlATELRNVNQSRQENDRRR 1292
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKADEAKKKAEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1293 KQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAElKASAAIKSAGNLEsQLTEAQQLLEEETRQKLAL 1372
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAK-KAEEAKKADEAKKAEEAKK 1535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1373 SSKLRQIESEKEALQEQLEEDeeAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAA 1452
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1453 NDRLDKSK-------KKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLS 1525
Cdd:PTZ00121 1614 KAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1526 LTRELDEAfEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEV 1605
Cdd:PTZ00121 1694 LKKEAEEA-KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 158285519 1606 NMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQ 1649
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1208-1974 |
1.07e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1208 SKREQEVATLKKTLEDESANHESTLMDMRHKhaqeisSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQE 1287
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK------TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1288 NDRRRKQAETQIAELQvkladvdrvRVELQDKVtklqQESENITQQLDEAELKASAAIKSAGnlESQLTEAQQLLEEETR 1367
Cdd:PTZ00121 1149 EDAKRVEIARKAEDAR---------KAEEARKA----EDAKKAEAARKAEEVRKAEELRKAE--DARKAEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1368 qklalSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQ 1447
Cdd:PTZ00121 1214 -----AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1448 ELQAANDRLDKSKKKIQSELEDA--TIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLS 1525
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1526 LTRELDEAFEKIDELetKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDdlqlTEDAKLRLEV 1605
Cdd:PTZ00121 1369 AEKKKEEAKKKADAA--KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK----ADEAKKKAEE 1442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1606 NMQALRAQferdiqakeEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKvKEDALKQA 1685
Cdd:PTZ00121 1443 AKKADEAK---------KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1686 KKLQAQIKDAIRDAEEAKAAKEELAAISKESERKvktlEADLMQLTEDLSSSERARRAAEGERDEllEEINSNSSKGSLM 1765
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEA 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1766 ideKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTElatEKSNSQNNETLKCGLERLNKELKAKLSEQETA 1845
Cdd:PTZ00121 1587 ---KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1846 LRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLD 1925
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1926 EAE---EEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKLSIHKDSKK 1974
Cdd:PTZ00121 1741 EDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
884-1606 |
3.73e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 95.21 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKLEN-----LSKNSQEYEKKYQQAMEEKTHLAEQLQA-----EIELCAEAEEGRARLVA 953
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDarkaeEARKAEDAKKAEAARKAEEVRKAEELRKaedarKAEAARKAEEERKAEEA 1217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 954 RKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQK-LQLEKVQLDAKLKKMEEdvaliedqN 1032
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEE--------K 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1033 HKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKlkvKHESTIAELEErLLKDHQQRQEADRSKRKIETEVADLKEQINER 1112
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKK---KAEEAKKKADA-AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1113 RMQIEEMQQQLVKREEEL---AQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLA--RSKAEKQKRDLNEELE 1187
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1188 AlkNELLDSLDTTAAQQELRSKREQEvatlKKTLEDESANHESTLMDMRHKHAQEISSINEQL---ENLKKMKGGLEKSK 1264
Cdd:PTZ00121 1446 A--DEAKKKAEEAKKAEEAKKKAEEA----KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaAEAKKKADEAKKAE 1519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1265 QQLEAENADLATELRNVNQSRQENDRR-----RKQAETQIAELQVKladVDRVRVELQDKVTKL-------QQESENITQ 1332
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKkadelKKAEELKKAEEKKK---AEEAKKAEEDKNMALrkaeeakKAEEARIEE 1596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1333 QLDEAELKASAAIKSAGNLESQLTEAQQLL-EEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTI 1411
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1412 QEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNF 1491
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1492 DKV---LAEEKAISEQVAQERDAAEREAREKETKVLSL-----TRELDEAFEKIDE--------LETKRKGLQNELDELA 1555
Cdd:PTZ00121 1757 KKIahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMevdkkIKDIFDNFANIIEggkegnlvINDSKEMEDSAIKEVA 1836
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 1556 NTQGTADKNVHELEKAKRALESQLAELKAQNEE-------LEDDLQLTEDAKLRLEVN 1606
Cdd:PTZ00121 1837 DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfnkekdlKEDDEEEIEEADEIEKID 1894
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1032-1950 |
5.06e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1032 NHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKvkheSTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINE 1111
Cdd:PTZ00121 1038 NDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLK----PSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1112 RRMQIEEMQQ-QLVKREEEL--AQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEA 1188
Cdd:PTZ00121 1114 ARKAEEAKKKaEDARKAEEArkAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEEL 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1189 LKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLE 1268
Cdd:PTZ00121 1194 RKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1269 AENADLATELRNVNQSRQENDRRRKQAETQIAELQVKlADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSA 1348
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1349 GNLESQL------TEAQQLLEEETRQKL------------ALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFT 1410
Cdd:PTZ00121 1353 EAAADEAeaaeekAEAAEKKKEEAKKKAdaakkkaeekkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1411 IQEMKKRSEEdsdiAKELEESKKKMN--KDIETLQRQIQELQAANDRLDKSKKKIQSEleDATIELDTQRTKVLELEKKQ 1488
Cdd:PTZ00121 1433 ADEAKKKAEE----AKKADEAKKKAEeaKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKADEAKKAA 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1489 KNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDE--AFEKIDELETKRKGLQNELDElaNTQGTADKNVH 1566
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAE 1584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1567 ELEKAKRALESQLAELKAQNEELE-DDLQLTEDAKLRLEvnmQALRAQFERDI--QAKEEQSEEKRRG--LVKALRDLEA 1641
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAE---ELKKAEEEKKKveQLKKKEAEEKKKAeeLKKAEEENKI 1661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1642 ELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDAlKQAKKLQAQIKDAIRDAEEAKAAkeelaaiskESERKVK 1721
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEAEEKKKAEELKKA---------EEENKIK 1731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1722 TLEADlMQLTEDLSSSERARRAaEGERDELLEEINSNSSKGSLMIDEKRrleariAALEEELEEEQSNLELMVDRNRKAQ 1801
Cdd:PTZ00121 1732 AEEAK-KEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKE------AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1802 LTIEQLTTElatekSNSQNNETLKCGLERLNKELKAKLSEQETALrtklkaataaSEAKNLNLEKQLENETKERLAVQKA 1881
Cdd:PTZ00121 1804 FDNFANIIE-----GGKEGNLVINDSKEMEDSAIKEVADSKNMQL----------EEADAFEKHKFNKNNENGEDGNKEA 1868
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1882 NRKLEKRIKE-LTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLE 1950
Cdd:PTZ00121 1869 DFNKEKDLKEdDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1073-1692 |
5.79e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 93.98 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1073 TIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLV---KREEELAQTLVRIDEESAAKAAAQK 1149
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEkleKEVKELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1150 TQRELESQLAEIQEDLEAEKLARSKAEKQKRDLnEELEALKNELLdsldttaAQQELRSKREQEVATLKKTLEDESANHE 1229
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYI-------KLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1230 STlmdmrHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQendRRRKQAETQIAELQVKLADV 1309
Cdd:PRK03918 325 GI-----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER---LKKRLTGLTPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1310 DRVRVELQDKVTKLQQESENITQQLDEAElKASAAIKSAgnlESQLTEAQQLLEEETRQKL--ALSSKLRQIESEKEALQ 1387
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELK-KAIEELKKA---KGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1388 EQLEEDEEAKTNYEKKLAElnftiqemKKRSEEDSDIAKELEESKKKMNK-DIETLQRQIQELQAANDRLDKSKKKIQSe 1466
Cdd:PRK03918 473 EKERKLRKELRELEKVLKK--------ESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKS- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1467 LEDATIELDTQRTKVLELEKKQKNFDKVLAEEKaiseqvaqerDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKG 1546
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELL----------KELEELGFESVEELEERLKELEPFYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1547 LQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEEL-EDDLQLTEDAKLRLEVNMQALRAQFErdiqakeeQS 1625
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELE--------EL 685
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1626 EEKRRGLVKALRDLEAELDEERKQRAAAVAakkkLEGDLKDMEA----TLEMNNKVKEDALKQAKKLQAQI 1692
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEElrekVKKYKALLKERALSKVGEIASEI 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
888-1451 |
1.64e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 888 QEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQaMEEKTHLAEQLQAEIElcaEAEEGRARLVARKQELEELMQDLES 967
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEIEELEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 968 RIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARqKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERAN 1047
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1048 DLS--QTLAEEEEKAKHLAKLKVKHES-----TIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMq 1120
Cdd:PRK03918 353 RLEelEERHELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1121 qqlvKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLdsldtt 1200
Cdd:PRK03918 432 ----KKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL------ 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1201 aaQQELRSKREQEVATLKKTLEDESANHESTLMDMRhKHAQEISSINEQLEN---LKKMKGGLEKSKQQLEAENADLATE 1277
Cdd:PRK03918 502 --AEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI-KLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1278 LRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAElkasaaiKSAGNLESQLTE 1357
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE-------KRLEELRKELEE 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1358 AQQLLEEET-----RQKLALSSKLRQIESEKEALqeqleedeeaktnyEKKLAELNFTIQEMKKRSEEDSDIAKELeESK 1432
Cdd:PRK03918 652 LEKKYSEEEyeelrEEYLELSRELAGLRAELEEL--------------EKRREEIKKTLEKLKEELEEREKAKKEL-EKL 716
|
570
....*....|....*....
gi 158285519 1433 KKMNKDIETLQRQIQELQA 1451
Cdd:PRK03918 717 EKALERVEELREKVKKYKA 735
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1028-1627 |
2.07e-17 |
|
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: 88.92 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1028 IEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKE 1107
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1108 QINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQlaeiQEDLEAEKLarsKAEKQKRDLNEELE 1187
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ----KEELENELN---LLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1188 ALKNELLDSLDTTAAQQelrsKREQEVATLKKTLEdESANHESTLMDMRHKHAQEISSINEQLENLkkmkgglEKSKQQL 1267
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLK----KKIQKNKSLESQIS-ELKKQNNQLKDNIEKKQQEINEKTTEISNT-------QTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1268 EAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVelQDKVTKLQQESENITQQLDEAELKASAAIKS 1347
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1348 AGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKE 1427
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1428 LEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQ 1507
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1508 ERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTAD--KNVHELEKAKRALESQLAELKAQ 1585
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQT 576
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 158285519 1586 NEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEE 1627
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
949-1281 |
3.29e-17 |
|
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: 88.59 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 949 ARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALI 1028
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1029 EDQNHKLVKEKKLLEERA-------NDLSQTLAEE--EEKAKHLAKLKVKH---ESTIAELEERLLKDHQQRQEADRSKR 1096
Cdd:TIGR02169 757 KSELKELEARIEELEEDLhkleealNDLEARLSHSriPEIQAELSKLEEEVsriEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1097 KIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAE 1176
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1177 KQKRDLNEELEALKNElLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHEsTLMDMRHKHAQEISSINEQLENLKKM 1256
Cdd:TIGR02169 917 KRLSELKAKLEALEEE-LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEK 994
|
330 340
....*....|....*....|....*
gi 158285519 1257 KGGLEKSKQQLEAENADLATELRNV 1281
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
904-1525 |
4.39e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 904 DKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEK 983
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 984 KKLQiniqdleeqleeeeaarqKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQtLAEEEEKAKHL 1063
Cdd:PRK03918 238 EEIE------------------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1064 AKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEqINERRMQIEEMQQQLVKREEELAQtlVRIDEESAA 1143
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEERHELYEE--AKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1144 KAAAQKTQRELEsqlaEIQEDLEAEKLARSKAEKQKRDLNEELEALKNElldSLDTTAAQQELRsKREQEVATLKKTLED 1223
Cdd:PRK03918 376 RLKKRLTGLTPE----KLEKELEELEKAKEEIEEEISKITARIGELKKE---IKELKKAIEELK-KAKGKCPVCGRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1224 EsanHESTLMDmrhKHAQEISSINEQLENLKKMKGGLEKSKQQLEAE---------NADLATELRNVNQSRQE-NDRRRK 1293
Cdd:PRK03918 448 E---HRKELLE---EYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKyNLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1294 QAETQIAELQVKLADVDRVRVELQDKVTKLQQ---ESENITQQLDEAELKASAAIKSAGNL----ESQLTEAQQLLEEET 1366
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1367 RQKLALSSKLRQIESEKEALQEQLEEDEEAktnyEKKLAELNFTIQEMKKRSEEDSDIAKElEESKKKMNKDIEtLQRQI 1446
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEELEKKYSE-EEYEELREEYLE-LSREL 675
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1447 QELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKkqknFDKVLAEEKAISEQVAQERDAAEREAREKETKVLS 1525
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELREKVKKYKALLKERALSKVGEIAS 750
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1148-1935 |
4.64e-17 |
|
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: 87.87 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1148 QKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESAN 1227
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1228 HESTLmdmrhkhaQEISSINEQLEnlkkmkgglEKSKQQLEAENADLATELRNVNQSRQENDRrrkQAETQIAELQVKLA 1307
Cdd:pfam15921 182 HEGVL--------QEIRSILVDFE---------EASGKKIYEHDSMSTMHFRSLGSAISKILR---ELDTEISYLKGRIF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1308 DVD----RVRVELQDKVTKL-QQESENITQQLDEAEL-------KASAAIKSAGNLESQLteaqQLLEEETRQKLALSsk 1375
Cdd:pfam15921 242 PVEdqleALKSESQNKIELLlQQHQDRIEQLISEHEVeitglteKASSARSQANSIQSQL----EIIQEQARNQNSMY-- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1376 LRQIESEKEALQEQLEEDEEAKTNYEKKLAEL-------NFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQE 1448
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELekqlvlaNSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1449 LQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKkqknfdkVLAEEKAISEQVAQERDAAEREAREKETKVLSLTR 1528
Cdd:pfam15921 396 EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA-------LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1529 ELDEAFEK----IDELETKRKGLQNeldelanTQGTADKNVHELEKAKRALESQLAELkaqneeleddlqltedAKLRLE 1604
Cdd:pfam15921 469 QLESTKEMlrkvVEELTAKKMTLES-------SERTVSDLTASLQEKERAIEATNAEI----------------TKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1605 VNmqaLRAQFERDIQAKEEQseekrrglvkaLRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQ 1684
Cdd:pfam15921 526 VD---LKLQELQHLKNEGDH-----------LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1685 AKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSL 1764
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1765 MIDEKRRLEARIAALEEELEEEQSNLELMVdrnRKAQLTIEQLTTELATEKSNSQNNETLKCGLErlnKELKAKLSeQET 1844
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQL---KSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ---KQITAKRG-QID 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1845 ALRTKLKAATAAseAKNLNLEKQLENETKERLAVQKANRKLEKriKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNL 1924
Cdd:pfam15921 745 ALQSKIQFLEEA--MTNANKEKHFLKEEKNKLSQELSTVATEK--NKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
810
....*....|.
gi 158285519 1925 DEAEEEIQKEK 1935
Cdd:pfam15921 821 AECQDIIQRQE 831
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1002-1650 |
4.26e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.97 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1002 AARQKLQLEK-VQLDAKLKKMEEDVALIEDQNHKLVKEKKllEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEER 1080
Cdd:COG4913 247 AREQIELLEPiRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1081 LLKDHQQRQEAD-RSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTlvrideesaaKAAAQKTQRELESQLA 1159
Cdd:COG4913 325 LDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS----------AEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1160 EIQEDLEAEKLARSKAEKQKRDLNEELEALKNELldsldttaaqQELRSKR---EQEVATLKKTLEDESANHEST----- 1231
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEI----------ASLERRKsniPARLLALRDALAEALGLDEAElpfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1232 -LMDMR------------------------HKHAQEISSINEQLenlkKMKGGL--------EKSKQQLEAENADLAT-- 1276
Cdd:COG4913 465 eLIEVRpeeerwrgaiervlggfaltllvpPEHYAAALRWVNRL----HLRGRLvyervrtgLPDPERPRLDPDSLAGkl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1277 ----------------------------ELRNVN-------QSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVT 1321
Cdd:COG4913 541 dfkphpfrawleaelgrrfdyvcvdspeELRRHPraitragQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1322 KLQQEsenitqqldeaelkasaaiksAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQeqleedeeaktnYE 1401
Cdd:COG4913 621 ELEEE---------------------LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS------------AE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1402 KKLAELnftiQEMKKRSEEDSDIAKELEESkkkmnkdIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKV 1481
Cdd:COG4913 668 REIAEL----EAELERLDASSDDLAALEEQ-------LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1482 LELEKKQK-----NFDKVLAE------EKAISEQVAQERDAAEREAREKETKVLSL-----------TRELDEAFEKIDE 1539
Cdd:COG4913 737 EAAEDLARlelraLLEERFAAalgdavERELRENLEERIDALRARLNRAEEELERAmrafnrewpaeTADLDADLESLPE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1540 LETKRKGLQNE--------LDELANTQGTADKN--VHELEKAKRALESQLAELkaqNEELEdDLQLTEDAKLRLEVN--- 1606
Cdd:COG4913 817 YLALLDRLEEDglpeyeerFKELLNENSIEFVAdlLSKLRRAIREIKERIDPL---NDSLK-RIPFGPGRYLRLEARprp 892
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1607 -------MQALRAQFERDIQAKEEQSEEK---RRGLVKALRDLEAELDEERKQR 1650
Cdd:COG4913 893 dpevrefRQELRAVTSGASLFDEELSEARfaaLKRLIERLRSEEEESDRRWRAR 946
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
888-1697 |
1.39e-15 |
|
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: 83.17 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 888 QEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDLE- 966
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEh 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 967 --SRIEEEEERVNALTSEKKKLQ-INIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLE 1043
Cdd:TIGR00606 260 nlSKIMKLDNEIKALKSRKKQMEkDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1044 ERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQ-EADRS--------KRKIETEVADLKEQINERRM 1114
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpFSERQiknfhtlvIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1115 QIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLE-----AEKLARSKAEKQKRDLNEELE-- 1187
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDrilelDQELRKAERELSKAEKNSLTEtl 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1188 -----ALKNELLDSLDTTAAQQELRSKREQEVATLKKT--LEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKG-- 1258
Cdd:TIGR00606 500 kkevkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwl 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1259 -GLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRvELQDKVTKLQQESENITQQLdeA 1337
Cdd:TIGR00606 580 hSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ-DEESDLERLKEEIEKSSKQR--A 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1338 ELKASAAIKSAG-------------------NLESQLTEAQQLLEEETR----QKLALSSKLRQIESEKEALQEQLEEDE 1394
Cdd:TIGR00606 657 MLAGATAVYSQFitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1395 EAKTNYEKKLAELNFTIQEMKKR-SEEDSDIAKE---------LEESKKKMNKDIETLQRQIQELQAANDR--------- 1455
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDiQRLKNDIEEQetllgtimpEEESAKVCLTDVTIMERFQMELKDVERKiaqqaaklq 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1456 ---LDKSKKKIQSELEDATIELDTQRTKVLELEK----KQKNFDKV------LAEEKAISEQVAQERDAAEREAREKETK 1522
Cdd:TIGR00606 817 gsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKliqdQQEQIQHLksktneLKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1523 VLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVH-ELEKAKRALESQLAELKAQNEELEDDlqlTEDAKL 1601
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQDG---KDDYLK 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1602 RLEVNMQALRAQFERDIQAKEEQSEEkrrglvkaLRDLEAELDEERKQRA--AAVAAKKKLEGDLKDMEATLEMNNK-VK 1678
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINED--------MRLMRQDIDTQKIQERwlQDNLTLRKRENELKEVEEELKQHLKeMG 1045
|
890
....*....|....*....
gi 158285519 1679 EDALKQAKKLQAQIKDAIR 1697
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENID 1064
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1013-1696 |
3.59e-15 |
|
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: 81.70 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1013 QLDAKLKKMEEDVALIEDQNHKLVKEKK-----LLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQ 1087
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1088 RQEAD----RSKRKIETEVADLKEQINE-RRM---QIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLA 1159
Cdd:pfam15921 308 ARNQNsmymRQLSDLESTVSQLRSELREaKRMyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1160 EIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDsldttaaqqelRSKREQEVATLKKTLEDESANHESTLMDM---R 1236
Cdd:pfam15921 388 KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQMERQMAAiqgK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1237 HKHAQEISSINEQLENLKKMkggLEKSKQQLEAENADLATELRNVNQ---SRQENDRRRKQAETQIAELQvkladvDRVR 1313
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEM---LRKVVEELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLR------SRVD 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1314 VELQDkVTKLQQESE---NITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQL 1390
Cdd:pfam15921 528 LKLQE-LQHLKNEGDhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLEL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1391 EEDEEAKTNYEKKLAELNFTIQEMkkrseedsdiakELEESKKkMNKDIETLqRQIQELQAANDRLDKSKKKIQSEL--- 1467
Cdd:pfam15921 607 QEFKILKDKKDAKIRELEARVSDL------------ELEKVKL-VNAGSERL-RAVKDIKQERDQLLNEVKTSRNELnsl 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1468 -EDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKG 1546
Cdd:pfam15921 673 sEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1547 LQNELDelantqgTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRL-------EVNMQALRAQFE--RD 1617
Cdd:pfam15921 753 LEEAMT-------NANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLkekvanmEVALDKASLQFAecQD 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1618 IQAKEEQsEEKRRGL-----VKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEM-------NNKVKEDALKQA 1685
Cdd:pfam15921 826 IIQRQEQ-ESVRLKLqhtldVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFlshhsrkTNALKEDPTRDL 904
|
730
....*....|.
gi 158285519 1686 KKLQAQIKDAI 1696
Cdd:pfam15921 905 KQLLQELRSVI 915
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
876-1630 |
4.37e-15 |
|
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: 81.56 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 876 YTKVKPLLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEA----EEGRARL 951
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkklqEEELKLL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 952 VARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQ---------------------------DLEEQLEEEEA-- 1002
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKkekeeieelekelkeleikreaeeeeeEELEKLQEKLEql 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1003 ----------ARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSqTLAEEEEKAKHLAKLKVKHES 1072
Cdd:pfam02463 372 eeellakkklESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL-EILEEEEESIELKQGKLTEEK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1073 TIAELEE--RLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKT 1150
Cdd:pfam02463 451 EELEKQElkLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1151 QRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHES 1230
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1231 TLMDM-----RHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVK 1305
Cdd:pfam02463 611 ATLEAdeddkRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1306 LADVDRVRVELQDKVTKLQQESENITQQLDE--AELKASAAIKSAGNLESQLTEAQQLLEEET------RQKLALSSKLR 1377
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEEllADRVQEAQDKINEELKLLKQKIDEEEEEEEksrlkkEEKEEEKSELS 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1378 QIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLD 1457
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1458 KSKKKIQSELEDATIELDTQRtkvlELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKI 1537
Cdd:pfam02463 851 LAEEELERLEEEITKEELLQE----LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1538 DELETKRKGLQNELDELANTQGTADKNVHELEKaKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERD 1617
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
810
....*....|...
gi 158285519 1618 IQAKEEQSEEKRR 1630
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
886-1369 |
4.77e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 886 TKQEEKLVQKEDELRQIRDKleNLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELmqdl 965
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 966 ESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLqLEKVQLDaklkkmEEDVALIEDQNHKLVKEKKLLEER 1045
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL-LAEAGLD------DADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1046 ANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVK 1125
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1126 REEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKL--------------ARSKAEKQKRDLNEELEALKN 1191
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsphveTIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1192 ElLDSLDTTAAQQELRSKREQEVATLK---KTLEDESANHESTLMDMRHKhaqeISSINEQLENLKKMKGGLEKSKQQLE 1268
Cdd:PRK02224 490 E-VEEVEERLERAEDLVEAEDRIERLEerrEDLEELIAERRETIEEKRER----AEELRERAAELEAEAEEKREAAAEAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1269 AENADLATELRNVNQSRQENDRRRKQAETqIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDE-----AELKAS- 1342
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEkrerkRELEAEf 643
|
490 500
....*....|....*....|....*....
gi 158285519 1343 --AAIKSAGNLESQLTEAQQLLEEETRQK 1369
Cdd:PRK02224 644 deARIEEAREDKERAEEYLEQVEEKLDEL 672
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
889-1588 |
7.73e-15 |
|
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: 80.86 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 889 EEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQaeielcaEAEEGRARLVARKQELEELMQDLEsr 968
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ-------QLEGSSDRILELDQELRKAERELS-- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 969 ieeeEERVNALTSEKKKLQINiqdleeqleeeeaarqkLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERAND 1048
Cdd:TIGR00606 489 ----KAEKNSLTETLKKEVKS-----------------LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1049 LSQTLAEEEEKAKHLAKLKVKHESTiAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREE 1128
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1129 ELAQTLVRIDEESAAKAAAQKTQRElESQLAEI--QEDLEAEKLARSKAEKQ------------KRDLNEELEALKNELL 1194
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKS-SKQRAMLagATAVYSQFITQLTDENQsccpvcqrvfqtEAELQEFISDLQSKLR 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1195 DSLDTTAAQQELRSKREQEVATLKKTLEDESanhesTLMDMRHKHAQEISSINEQLE-NLKKMKGGLEKSKQQLEAENA- 1272
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRQ-----SIIDLKEKEIPELRNKLQKVNrDIQRLKNDIEEQETLLGTIMPe 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1273 -----DLATELRNVNQSRQENDRRRKQAETQIAELQVklADVDRVRVELQDKVTKLQQESENITQQLDEAelkasaaiks 1347
Cdd:TIGR00606 781 eesakVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQHELDTVVSKIELN---------- 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1348 agnlesqlteaQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKE 1427
Cdd:TIGR00606 849 -----------RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1428 LEeskKKMNKDIETLQRQIQELQAANDRLDKSKKKIQS------------------ELEDATIELDTQRTKVLELEKKQK 1489
Cdd:TIGR00606 918 LE---KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdienkiqdgkddYLKQKETELNTVNAQLEECEKHQE 994
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1490 NFDKVL-AEEKAISEQVAQER---DAAEREAREKETKVLSLTRE--LDEAFE-KIDELETKRKGLQNELDELANTQGTAD 1562
Cdd:TIGR00606 995 KINEDMrLMRQDIDTQKIQERwlqDNLTLRKRENELKEVEEELKqhLKEMGQmQVLQMKQEHQKLEENIDLIKRNHVLAL 1074
|
730 740
....*....|....*....|....*.
gi 158285519 1563 KNVHELEKAKRALESQLAELKAQNEE 1588
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKELREPQFRDAE 1100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
938-1759 |
1.24e-14 |
|
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: 80.02 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 938 IELCAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQ----INIQDLEEQLEEEEAARQKLQLEKVQ 1013
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1014 LDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLS---QTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQE 1090
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1091 ADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLvrideesaakaaaqKTQRELESQLAEIQEDLEAEKL 1170
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE--------------KLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1171 ARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLED------ESANHESTLMDMRHKHAQEIS 1244
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEEsielkqGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1245 SINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQ 1324
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1325 QESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKL 1404
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1405 AELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLEL 1484
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1485 EKKQKNFDKVLAEEKAISEQVAQER--DAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELAnTQGTAD 1562
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEaqDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA-EEREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1563 KNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAE 1642
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1643 LDEERKQRaAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKT 1722
Cdd:pfam02463 864 TKEELLQE-LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
810 820 830
....*....|....*....|....*....|....*..
gi 158285519 1723 LEADLMQLTEDLSSSERARRAAEGERDELLEEINSNS 1759
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMA 979
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
842-1545 |
1.50e-14 |
|
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: 79.38 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 842 RNYQKRLQQLNAIRIIQRNCAAYLKLRNwqwwrlyTKVKPLLEVTKQEEK-LVQKEDELRQIRDKLENLSKNSQEYEKKY 920
Cdd:pfam05483 102 KQKENKLQENRKIIEAQRKAIQELQFEN-------EKVSLKLEEEIQENKdLIKENNATRHLCNLLKETCARSAEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 921 QQAMEEKTHLAEQLQAEIE--------LCAEAEEGRARLVARKQELEELMQDLEsriEEEEERVNALTSEKKKLQINIQD 992
Cdd:pfam05483 175 EYEREETRQVYMDLNNNIEkmilafeeLRVQAENARLEMHFKLKEDHEKIQHLE---EEYKKEINDKEKQVSLLLIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 993 LEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEK---KLLEERANDLSQTLAEEEEKAKhlaklkvk 1069
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELediKMSLQRSMSTQKALEEDLQIAT-------- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1070 heSTIAELEErllKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQK 1149
Cdd:pfam05483 324 --KTICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1150 TQRELESQLAEIQEDLeAEKLARSKAEKQKRDLNEELEALKNELLDSLDTtaaqqelrskREQEVATLKKTLEDESANHE 1229
Cdd:pfam05483 399 FKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQA----------REKEIHDLEIQLTAIKTSEE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1230 STLMDMRHKHAQeisSINEQLEN--LKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLA 1307
Cdd:pfam05483 468 HYLKEVEDLKTE---LEKEKLKNieLTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1308 DVdrvRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQ 1387
Cdd:pfam05483 545 NL---RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALK 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1388 EQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNkdiETLQRQIQELQAANDRLDKSKKKIQSEL 1467
Cdd:pfam05483 622 KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE---EKLLEEVEKAKAIADEAVKLQKEIDKRC 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1468 EDATIELdtqrtkVLELEKKQKNFDKVLAEE-------KAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDEL 1540
Cdd:pfam05483 699 QHKIAEM------VALMEKHKHQYDKIIEERdselglyKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
....*
gi 158285519 1541 ETKRK 1545
Cdd:pfam05483 773 KMEAK 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1093-1497 |
3.40e-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: 78.57 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1093 RSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLAR 1172
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1173 SKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDEsanhestlmdmrhkhaqEISSINEQLEn 1252
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS-----------------RIPEIQAELS- 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1253 lkkmkgglekskqQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQ 1332
Cdd:TIGR02169 802 -------------KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1333 QLDEAELKASAAIKSAGNLESQLTEAQQLLEEetrqklaLSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQ 1412
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRE-------LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1413 EMKKRSEEDSDIAKeLEESKKKMNKDIETLQ----RQIQELQAANDRLDKSKKKIQ------SELEDATIELDTQRTKVL 1482
Cdd:TIGR02169 942 EDEEIPEEELSLED-VQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAkleeerKAILERIEEYEKKKREVF 1020
|
410
....*....|....*..
gi 158285519 1483 --ELEKKQKNFDKVLAE 1497
Cdd:TIGR02169 1021 meAFEAINENFNEIFAE 1037
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1096-1698 |
3.52e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.42 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1096 RKIETEVADLKEQInERRMQIEEMQQQLVKREEELAQtlVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKA 1175
Cdd:COG4913 238 ERAHEALEDAREQI-ELLEPIRELAERYAAARERLAE--LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1176 EKQKRDLNEELEALKNELLDS-----------LDTTAAQQELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEIS 1244
Cdd:COG4913 315 EARLDALREELDELEAQIRGNggdrleqlereIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1245 SINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSR----QENDRRRKQ--AETQIAE---------LQVKLAD- 1308
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDAlaEALGLDEaelpfvgelIEVRPEEe 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1309 ------------------------------VDRVRVELQ---DKVTKLQQESEniTQQLDEAELkasaaiksAGNLESQL 1355
Cdd:COG4913 475 rwrgaiervlggfaltllvppehyaaalrwVNRLHLRGRlvyERVRTGLPDPE--RPRLDPDSL--------AGKLDFKP 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1356 TEAQQLLEEEtrqkLALSSKLRQIESEKEALqeqleedeeaktNYEKK-----LAELNFTIQEMKKRSEEDSD------- 1423
Cdd:COG4913 545 HPFRAWLEAE----LGRRFDYVCVDSPEELR------------RHPRAitragQVKGNGTRHEKDDRRRIRSRyvlgfdn 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1424 IAKeleeskkkmnkdIETLQRQIQELQAandrldkskkkiqseledatiELDTQRTKVLELEKKQKNFDKVLAEEKAISE 1503
Cdd:COG4913 609 RAK------------LAALEAELAELEE---------------------ELAEAEERLEALEAELDALQERREALQRLAE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1504 QVAQERD--AAEREAREKETKVlsltRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAE 1581
Cdd:COG4913 656 YSWDEIDvaSAEREIAELEAEL----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1582 LKAQNEELEDDLQLTEDAKL---RLEVNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKqraaavAAKK 1658
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLeerFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWP------AETA 805
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1659 KLEGDLKDMEATLEMNNKVKEDALKQAKK----------------LQAQIKDAIRD 1698
Cdd:COG4913 806 DLDADLESLPEYLALLDRLEEDGLPEYEErfkellnensiefvadLLSKLRRAIRE 861
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1305-1909 |
8.41e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1305 KLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEaqqlLEEETRQKLALSSKLRQIESEKE 1384
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE----LREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1385 ALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMnKDIETLQRQIQELQAANDRLDKSKKKIQ 1464
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1465 SELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKR 1544
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1545 KGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNmqalraqferDIQAKEEQ 1624
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELK----------RIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1625 SEEKRRGLVKALRDLEAELDEERKQRAAAV--AAKKKLEGDLKDMEA-TLEMNNKVKEDALKQAKKLQAQIKDAIRDAEE 1701
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1702 AKAAKEELAAIskesERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEE 1781
Cdd:PRK03918 551 LEELKKKLAEL----EKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1782 ELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKcglerlnkelkakLSEQETALRTKLKAATAASEAKN 1861
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE-------------LSRELAGLRAELEELEKRREEIK 693
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 158285519 1862 LNLEKqLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQ 1909
Cdd:PRK03918 694 KTLEK-LKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
937-1547 |
3.02e-13 |
|
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: 75.65 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 937 EIELCAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLeeeeaaRQKLQLEKVQLDA 1016
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1017 KLKKMEEDVALIEDQnhKLVKEKKLLEERANDLSQT---LAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQ------ 1087
Cdd:pfam12128 316 AVAKDRSELEALEDQ--HGAFLDADIETAAADQEQLpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdia 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1088 ---------RQEADRSKRKIEtevADLKEQINERRmqiEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELEsQL 1158
Cdd:pfam12128 394 gikdklakiREARDRQLAVAE---DDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLL-QL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1159 AEIQEDLEAEKLARSKAEKQKRDLNEELEALK---NELLDSL-DTTAAQQELRSKREQ-------EVATLKKTLEDESAN 1227
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEVERLQSELRQARkrrDQASEALrQASRRLEERQSALDElelqlfpQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1228 HE--------STLMDMRHKHAQEISSINEQLENLKKMKGGLEK--------SKQQLEAENADLATELRNVNQSRQENDRR 1291
Cdd:pfam12128 547 WEqsigkvisPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpewaaSEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1292 RKQAETQIAELQVKLADVDRV----RVELQDKVTKLQQESENITQQLDEAELKASAAIKS-AGNLESQLTEAQQLLEEET 1366
Cdd:pfam12128 627 LVQANGELEKASREETFARTAlknaRLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSlEAQLKQLDKKHQAWLEEQK 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1367 RQKL---------------ALSSKLRQIESEKEALQEQLEEDEEA-KTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEE 1430
Cdd:pfam12128 707 EQKReartekqaywqvvegALDAQLALLKAAIAARRSGAKAELKAlETWYKRDLASLGVDPDVIAKLKREIRTLERKIER 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1431 SKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQ----RTKVLELEKKQKNFDKVLAEekaISEQVA 1506
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLiadtKLRRAKLEMERKASEKQQVR---LSENLR 863
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 158285519 1507 QERDAAEREAREKE-TKVLSLTRELDEAFEKIDELETKRKGL 1547
Cdd:pfam12128 864 GLRCEMSKLATLKEdANSEQAQGSIGERLAQLEDLKLKRDYL 905
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
895-1608 |
3.96e-13 |
|
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: 74.67 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 895 KEDELRQIRDKLENLSKNSQEYEKKyqqameekthlaeqlqaeielcaeaeegrarlvarKQELEELMQDLESRIEEEEE 974
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENE-----------------------------------LNLLEKEKLNIQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 975 RVNALTSEKKKLQINIQdleeqleeeeaarqklqlekvqldaKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLA 1054
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQ-------------------------KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1055 EEEEKakhLAKLKVKHESTIAELEERllkdhqqRQEADRSKRKIEtevaDLKEQINERRMQIEEMQQQlvkreeelaqtl 1134
Cdd:TIGR04523 250 NTQTQ---LNQLKDEQNKIKKQLSEK-------QKELEQNNKKIK----ELEKQLNQLKSEISDLNNQ------------ 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1135 vrideesaakaAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEV 1214
Cdd:TIGR04523 304 -----------KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1215 ATLKKtlEDESANHESTlmdmrhKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQ 1294
Cdd:TIGR04523 373 EKLKK--ENQSYKQEIK------NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1295 AETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDeaelkasaaiksagNLESQLTEAQQLLEEETRQKLALSS 1374
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE--------------QKQKELKSKEKELKKLNEEKKELEE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1375 KLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDsdiakELEESKKKMNKDIETLQRQIQELQAAND 1454
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE-----NLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1455 RLDKSKKKIQSELEDATIELDTQRTKVLELEKKqknFDKVLAEEKAISEQVAQERDAAErearEKETKVLSLTRELDEAF 1534
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE---LEKAKKENEKLSSIIKNIKSKKN----KLKQEVKQIKETIKEIR 658
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1535 EKIDELETKRKGLQNELDELANTQGTADK--NVHELEKAKRALESQ-LAELKAQNEELEDDLQLTEDAKLRLEVNMQ 1608
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDDIIELMKDWLKelSLHYKKYITRMIRIKdLPKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1345-1944 |
6.55e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1345 IKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNY----------EKKLAELNFTIQEM 1414
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeelekeleslEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1415 KKRSEEDSDIAKELEESKKKMNKdIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKV 1494
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1495 LAEEKAISEQVA--QERDAAEREAREKETKVLSLTREL-----DEAFEKIDELETKRKGLQNELDELANTQGTADKNVHE 1567
Cdd:PRK03918 344 KKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1568 LEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNmqalraqferDIQAKEEQSEEKRRGLVKALRDLEAELDEER 1647
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELK----------RIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1648 KQRAAAV--AAKKKLEGDLKDMEA-TLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAIskesERKVKTLE 1724
Cdd:PRK03918 494 ELIKLKElaEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL----EKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1725 ADLMQLTEDLsssERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIaaleeeleeeqsnlelmvDRNRKAQLTI 1804
Cdd:PRK03918 570 EELAELLKEL---EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREE------------------KELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1805 EQLTTELATEKSNsqnnetlkcgLERLNKELKAKLSEqetalrtklkaataASEAKNLNLEKQLENETKERLAVQKANRK 1884
Cdd:PRK03918 629 DKAFEELAETEKR----------LEELRKELEELEKK--------------YSEEEYEELREEYLELSRELAGLRAELEE 684
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1885 LEKRIKELTMNIEDERRHadqyKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRE 1944
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
883-1270 |
9.61e-13 |
|
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: 73.52 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 883 LEVTKQEEKLVQKEDELRQIRDKLENLSKN-SQEYEKKYQQAMEEKTHLAEQLQAEIelcAEAEEgrarlvaRKQELEEL 961
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQI---SQNNK-------IISQLNEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 962 MQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKL 1041
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1042 LEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQ 1121
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1122 QLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEK--LARSKAEKQKRDLNEELEALKNELLDSLDT 1199
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1200 TAAQQELRSKREQEVATLKKTLEdesanhesTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAE 1270
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIE--------EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
978-1671 |
1.77e-12 |
|
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: 72.83 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 978 ALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLkkmEEDValieDQNHKLVKEKKLLEERANDLSQTLAEEE 1057
Cdd:pfam05483 96 SIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKL---EEEI----QENKDLIKENNATRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1058 EKAKHLAKLKVKHESTIAEL----EERLLKDHQQRQEADRSKRKIETEVADLKEQINERRmqiEEMQQQLVKREEELAQT 1133
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLnnniEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLE---EEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1134 LVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQE 1213
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1214 VATLkkTLEDESANHESTLMDMRHKHA-QEISSINEQLENL-KKMKGGLEKSKQQLEAenadLATELRNVNQSRQENDRR 1291
Cdd:pfam05483 326 ICQL--TEEKEAQMEELNKAKAAHSFVvTEFEATTCSLEELlRTEQQRLEKNEDQLKI----ITMELQKKSSELEEMTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1292 RKQAETQIAELQVKLAD----------VDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQL 1361
Cdd:pfam05483 400 KNNKEVELEELKKILAEdeklldekkqFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1362 LEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKlaelnftIQEMKKRSEEDSDIAKELEESKKKMNKDIET 1441
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED-------IINCKKQEERMLKQIENLEEKEMNLRDELES 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1442 LQRQ-IQELQAANDRLDKSK---KKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAR 1517
Cdd:pfam05483 553 VREEfIQKGDEVKCKLDKSEenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1518 EKETKVLSLTRELDEAFEKIDEL--------ETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEEL 1589
Cdd:pfam05483 633 AYEIKVNKLELELASAKQKFEEIidnyqkeiEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKH 712
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1590 E---DDLQLTEDAKLRLEVNmqalraqferdiqaKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKD 1666
Cdd:pfam05483 713 KhqyDKIIEERDSELGLYKN--------------KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
....*
gi 158285519 1667 MEATL 1671
Cdd:pfam05483 779 NTAIL 783
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1399-1974 |
4.41e-12 |
|
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: 71.59 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1399 NYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELqaaNDRLDKSKKKIQSELEDATI---ELD 1475
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDL---NDKLKKNKDKINKLNSDLSKinsEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1476 TQRTKVLELEKKQKNFDKVLAEEKAISEQVAQErdaaereAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELA 1555
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1556 NTQGTADK----------NVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFerdIQAKEEQS 1625
Cdd:TIGR04523 187 KNIDKIKNkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL---NQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1626 EEKRrglvkalrdleaELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALkqAKKLQAQIKDAIRDAEEAKAA 1705
Cdd:TIGR04523 264 KIKK------------QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1706 KEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEE 1785
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1786 EQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQETalrtKLKAATAASEAKNLNLE 1865
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET----QLKVLSRSINKIKQNLE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1866 ---KQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKE--KTLKRK 1940
Cdd:TIGR04523 486 qkqKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDE 565
|
570 580 590
....*....|....*....|....*....|....
gi 158285519 1941 AQRECEDMLESHEALSREVNALKSKLSIHKDSKK 1974
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
882-1364 |
6.42e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 882 LLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKkyqqameekthLAEQLQAEIELCAEAEEGRARLVARKQELEEL 961
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-----------LSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 962 MQDLESRieeeEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKL----QLEKVQLDAKLKKMEEDVALIEDQNHKLVK 1037
Cdd:PRK03918 330 IKELEEK----EERLEELKKKLKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1038 EKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEErllkdhqqrQEADRSKRKIETEVADLKEQINErrmqIE 1117
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE---------EHRKELLEEYTAELKRIEKELKE----IE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1118 EMQQQLVKREEELAQTLVRIDEESaakaaaqkTQRELESQLAEIQEDLE---AEKLarSKAEKQKRDLNEELEALKNELL 1194
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELI--------KLKELAEQLKELEEKLKkynLEEL--EKKAEEYEKLKEKLIKLKGEIK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1195 DSLDTTAAQQELRSKREqEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADL 1274
Cdd:PRK03918 543 SLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1275 ATELRNVNQSRQENDRRRKQAE---TQIAELQVKLADVDRVRVElqDKVTKLQQESENITQQLDEAELKASAAIKSAGNL 1351
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEelrKELEELEKKYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
490
....*....|...
gi 158285519 1352 ESQLTEAQQLLEE 1364
Cdd:PRK03918 700 KEELEEREKAKKE 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
883-1545 |
6.66e-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: 71.15 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 883 LEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQamEEKTHlaEQLQAEIELCAEAeegrARLVARKQELEELM 962
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRA--QEAVL--EETQERINRARKA----APLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 963 QDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKvqldaKLKKMEEDVALIEDQNHKlvkeKKLL 1042
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI-----HIRDAHEVATSIREISCQ----QHTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1043 EERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEvadlKEQINERRMQIEEMQQQ 1122
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ----QRYAELCAAAITCTAQC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1123 LVKREEELAQTLVRIDEESAAKAAAQ------KTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDS 1196
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEqihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1197 LDTTAAQQELRSKREQEVATLKKTLEDESANHEStLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQleaenadlat 1276
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE-IQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK---------- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1277 ELRNVNQSRQENDRRRKQAETQIAELQVKLADvDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIK--SAGNLESQ 1354
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHL-QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPkeLLASRQLA 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1355 LTEAQQLLEEETRQKLALS---SKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIA-KELEE 1430
Cdd:TIGR00618 682 LQKMQSEKEQLTYWKEMLAqcqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlKARTE 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1431 SKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSeledatielDTQRTKVLELEKKQKnFDKVLAEEKAISEQVAQERD 1510
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE---------DTHLLKTLEAEIGQE-IPSDEDILNLQCETLVQEEE 831
|
650 660 670
....*....|....*....|....*....|....*
gi 158285519 1511 AAEREAREKETKVLSLTRELDEAFEKIDELETKRK 1545
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1422-1966 |
8.20e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1422 SDIAKELEESKKK-MNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKvLAEEKA 1500
Cdd:PRK02224 190 DQLKAQIEEKEEKdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED-LRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1501 ISEQvaqERDAAEREAREKETKVLSLTRELDEAF--------------EKIDELETKRKGLQNELDELANTQGTADKNVH 1566
Cdd:PRK02224 269 ETER---EREELAEEVRDLRERLEELEEERDDLLaeaglddadaeaveARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1567 ELEKAKRALESQLAELKAQNEELEDDLQLTEDAklrlevnmqalRAQFERDIQAKEEQSEEKRrglvKALRDLEAELDEE 1646
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREA-----------VEDRREEIEELEEEIEELR----ERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1647 RKQRAAAVAAKKKLEGDLKDMEATLemnnKVKEDALKQAKKLQAQIK-----DAIRDAEEAKAAKeelaaiskESERKVK 1721
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATL----RTARERVEEAEALLEAGKcpecgQPVEGSPHVETIE--------EDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1722 TLEADLMQLTEDLSSSE----RARRAAEGERD-ELLEEINSNSSKgslMIDEKR-RLEARiaaleeeleeeqsnlelmvd 1795
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEerleRAEDLVEAEDRiERLEERREDLEE---LIAERReTIEEK-------------------- 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1796 rnrkaQLTIEQLTTELAteksnsqnnetlkcglerlnkELKAKLSEQETALRTK-LKAATAASEAKNLNLEKQLENETKE 1874
Cdd:PRK02224 536 -----RERAEELRERAA---------------------ELEAEAEEKREAAAEAeEEAEEAREEVAELNSKLAELKERIE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1875 RLA----VQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAE-EEIQKEKTLKRKAQRECEDML 1949
Cdd:PRK02224 590 SLErirtLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKL 669
|
570 580
....*....|....*....|.
gi 158285519 1950 ----ESHEALSREVNALKSKL 1966
Cdd:PRK02224 670 delrEERDDLQAEIGAVENEL 690
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
906-1370 |
9.48e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 906 LENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKK 985
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 986 LQIniqdleeqLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAK 1065
Cdd:COG4717 128 LPL--------YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1066 LKVKHESTIAELEERL--LKDHQQRQEADRSKRKIETEVADLKEQINERRMQIE----------EMQQQLVKREEELAQT 1133
Cdd:COG4717 200 ELEELQQRLAELEEELeeAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallgLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1134 LVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQE 1213
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1214 VATLKktlEDESANHESTLMDMRH-KHAQEISSINEQLENLKKMKGGLEKSKQQLEAEN------------ADLATELRN 1280
Cdd:COG4717 360 EEELQ---LEELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLgeleellealdeEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1281 VNQSRQENDRRRKQAETQIAELQVKLAdvdrvRVELQDKVTKLQQESENITQQLDEAELKAsAAIKSAGNLesqLTEAQQ 1360
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELE-----QLEEDGELAELLQELEELKAELRELAEEW-AALKLALEL---LEEARE 507
|
490
....*....|
gi 158285519 1361 LLEEETRQKL 1370
Cdd:COG4717 508 EYREERLPPV 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1242-1937 |
1.07e-11 |
|
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: 70.05 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1242 EISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVT 1321
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1322 KLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYE 1401
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1402 KKLAELNFTIQEMKKRSEEDSDIAKE---LEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQR 1478
Cdd:TIGR04523 201 LLLSNLKKKIQKNKSLESQISELKKQnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1479 TKVLELEKKQKNFDKVLAEEKAISEQVAQERdaAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQ 1558
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISDLNNQKEQDWNKE--LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1559 GTADKnvhELEKAKRALESqlaeLKAQNEELEDDLQltedaklRLEVNMQALRAQFErDIQAKEEQSEEKRRGLVKALRD 1638
Cdd:TIGR04523 359 SEKQR---ELEEKQNEIEK----LKKENQSYKQEIK-------NLESQINDLESKIQ-NQEKLNQQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1639 LEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDaeeakaakeelaaiSKESER 1718
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN--------------LEQKQK 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1719 KVKTLEADLMQLTEdlssserarraaegERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNR 1798
Cdd:TIGR04523 490 ELKSKEKELKKLNE--------------EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1799 KAQLtieqlttelatEKSNSQNNETLKcGLERLNKELKAKLSEQETALRTKlkaataasEAKNLNLEKQLENETKERLAV 1878
Cdd:TIGR04523 556 KENL-----------EKEIDEKNKEIE-ELKQTQKSLKKKQEEKQELIDQK--------EKEKKDLIKEIEEKEKKISSL 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1879 QKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTL 1937
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
892-1695 |
1.63e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.00 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 892 LVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHL-AEQLQAEIeLCAEAEEGRARLVARKQELEELMQDLESRIE 970
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAeLLTLRSQL-LTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 971 EEEERVNALTSEKKKLQiniqdleeqleeeeaARQKLQLEKVQLDAKLKKMEEDVALIEDQNhklvkekklleerandls 1050
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQE---------------EQLKKQQLLKQLRARIEELRAQEAVLEETQ------------------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1051 qtlaEEEEKAKHLAKLkVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQiEEMQQQLVKREEEL 1130
Cdd:TIGR00618 284 ----ERINRARKAAPL-AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1131 AQTlvriDEESAAKAAAQKTQRELESQLAEIQEDLEAeklarskAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSkr 1210
Cdd:TIGR00618 358 RDA----HEVATSIREISCQQHTLTQHIHTLQQQKTT-------LTQKLQSLCKELDILQREQATIDTRTSAFRDLQG-- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1211 eqevatlkktledesanhestlmDMRHKHAQEISSineqlenlkkmkgglEKSKQQLEAENADLATELRNVNQSRQENDR 1290
Cdd:TIGR00618 425 -----------------------QLAHAKKQQELQ---------------QRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1291 RRKQAETQIAELQVKLADVDRVRvELQDKVTKLQQESEnitQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKL 1370
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKK-AVVLARLLELQEEP---CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1371 ALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQ 1450
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1451 AANDRLDKSKKKIQSELEDATIELDTQRTkvlELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTREL 1530
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHAL---QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1531 DEAFEKIDELETKRKGLQNELDELANTQGTADKNV-HELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQA 1609
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLaAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1610 LrAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDE--------------ERKQRAAAVAAKKKLEGDLKDMEATLEMNN 1675
Cdd:TIGR00618 780 L-SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdedilnlqcetlvqEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
810 820
....*....|....*....|
gi 158285519 1676 KVKEDALKQAKKLQAQIKDA 1695
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1483-1947 |
1.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1483 ELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELAntqgtAD 1562
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1563 KNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEvNMQALRAQFERDIQAKEEQSEEKRRglvKALRDLEAE 1642
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATE---EELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1643 LDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKT 1722
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1723 LEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKgslmidEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQL 1802
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE------ELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1803 TIEQLTTELATEKSnsqnnetlkcgLERLNKELKAKLSEQETALRTKLKAATAASEAKNL--NLEKQLENETKERLAVQK 1880
Cdd:COG4717 355 EAEELEEELQLEEL-----------EQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEleELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1881 ANRK--LEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNlDEAEEEIQKEKTLKRKAQRECED 1947
Cdd:COG4717 424 ALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1683-1966 |
2.18e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1683 KQAKKLQAQIKdaIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKG 1762
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1763 SLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQ 1842
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1843 ETALRTKLKAATAASEAKnLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKR 1922
Cdd:COG1196 371 EAELAEAEEELEELAEEL-LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 158285519 1923 NLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKL 1966
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1282-1512 |
3.38e-11 |
|
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: 67.48 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1282 NQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQL 1361
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1362 LEEetrQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIET 1441
Cdd:COG4942 99 LEA---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1442 LQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAA 1512
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
883-1598 |
4.02e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.61 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 883 LEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIElcaEAeegrarlvarKQELEELM 962
Cdd:pfam15921 278 VEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELR---EA----------KRMYEDKI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 963 QDLESRIEEEEERVNALTSEkkklqiniqdleeqleeeeaaRQKLQLEKVQLDAKLKKMEEDValiedqnHKLVKEkkll 1042
Cdd:pfam15921 345 EELEKQLVLANSELTEARTE---------------------RDQFSQESGNLDDQLQKLLADL-------HKREKE---- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1043 eerandlsqtLAEEEEKAKHLAKLKVKHESTIaeleerllkDHQQRQEADRSKrKIETEVADLKEQINERRMQIEEMQQQ 1122
Cdd:pfam15921 393 ----------LSLEKEQNKRLWDRDTGNSITI---------DHLRRELDDRNM-EVQRLEALLKAMKSECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1123 LVKREEELaqtlvridEESAAKAAAQKTQRELesqLAEIQEDLEAEKLARSKAEKQKRDLNEELEAlKNELLDSldTTAA 1202
Cdd:pfam15921 453 IQGKNESL--------EKVSSLTAQLESTKEM---LRKVVEELTAKKMTLESSERTVSDLTASLQE-KERAIEA--TNAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1203 QQELRSKREQEVATLK--KTLEDESANHESTLMDMRHKHAQE---ISSINEQLENLKKMKGGLEKSKQQLEAENADLATE 1277
Cdd:pfam15921 519 ITKLRSRVDLKLQELQhlKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1278 LRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEaelkASAAIKSAGNLESQLTE 1357
Cdd:pfam15921 599 INDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ----LLNEVKTSRNELNSLSE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1358 AQQLLEEETRQKlalssklrqieseKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNK 1437
Cdd:pfam15921 675 DYEVLKRNFRNK-------------SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1438 DIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTkvlELEKKQKNFDKVLAEEKAISEQVAQERDAAER--- 1514
Cdd:pfam15921 742 QIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVAT---EKNKMAGELEVLRSQERRLKEKVANMEVALDKasl 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1515 ---------EAREKETKVLSLTRELDeafekIDELE----TKRKGLQNEL----------DELANTQGTADKNVHELEKA 1571
Cdd:pfam15921 819 qfaecqdiiQRQEQESVRLKLQHTLD-----VKELQgpgyTSNSSMKPRLlqpasftrthSNVPSSQSTASFLSHHSRKT 893
|
730 740 750
....*....|....*....|....*....|....*
gi 158285519 1572 K-------RALESQLAELKAQ-NEELEDDLQLTED 1598
Cdd:pfam15921 894 NalkedptRDLKQLLQELRSViNEEPTVQLSKAED 928
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
884-1344 |
6.06e-11 |
|
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: 67.94 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDElrQIRDKLENL-SKNSQEYEKKYQQAMEEKTHLaEQLQAEIelcaeaeegRARLVARKQELEELM 962
Cdd:pfam12128 372 DVTAKYNRRRSKIKE--QNNRDIAGIkDKLAKIREARDRQLAVAEDDL-QALESEL---------REQLEAGKLEFNEEE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 963 QDLESRIEEEEERVNALT-SEKKKLQINIQDLE-----EQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLV 1036
Cdd:pfam12128 440 YRLKSRLGELKLRLNQATaTPELLLQLENFDERierarEEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1037 KEKKLLEERANDLSQTLAE---------EEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIET-EVADLK 1106
Cdd:pfam12128 520 SALDELELQLFPQAGTLLHflrkeapdwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVpEWAASE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1107 EQINERRMQIEEM---QQQLVKR-EEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLA--------RSK 1174
Cdd:pfam12128 600 EELRERLDKAEEAlqsAREKQAAaEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKknkalaerKDS 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1175 AEKQKRDLNEELEALKNELLDSLDTTAAQ-QELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENL 1253
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1254 KKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDR-RRKQAETQIAE---LQVKLADVDRVRVELQDKVTKLQQESEN 1329
Cdd:pfam12128 760 LASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyFDWYQETWLQRrprLATQLSNIERAISELQQQLARLIADTKL 839
|
490
....*....|....*
gi 158285519 1330 ITQQLdEAELKASAA 1344
Cdd:pfam12128 840 RRAKL-EMERKASEK 853
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1259-1966 |
6.56e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.84 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1259 GLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEA- 1337
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTv 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1338 -ELKASAAIKsagnlESQLTEAQQLLEEETRQKLALSSKLRQIES-----EKEALQEQLEEDEEAKTNYE-------KKL 1404
Cdd:pfam15921 152 hELEAAKCLK-----EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvdfEEASGKKIYEHDSMSTMHFRslgsaisKIL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1405 AELNFTIQEMKKRSEEDSDiakELEESKKKMNKDIETLqrqiqeLQAANDRLDKSKKKIQSELEDATIELDTQRTKVlel 1484
Cdd:pfam15921 227 RELDTEISYLKGRIFPVED---QLEALKSESQNKIELL------LQQHQDRIEQLISEHEVEITGLTEKASSARSQA--- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1485 ekkqknfDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAF----EKIDELETKRKGLQNEL-------DE 1553
Cdd:pfam15921 295 -------NSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKrmyeDKIEELEKQLVLANSELtearterDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1554 LANTQGTADKNVHELEKAKRALESQLAELKAQNEELED--------------DLQLTEDAKLRLEVNMQALRA----QFE 1615
Cdd:pfam15921 368 FSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsitidhlrrELDDRNMEVQRLEALLKAMKSecqgQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1616 RD---IQAKEEqSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQI 1692
Cdd:pfam15921 448 RQmaaIQGKNE-SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1693 KDAIRDAEEAKAAKEELAAISKESE----------RKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNS--- 1759
Cdd:pfam15921 527 DLKLQELQHLKNEGDHLRNVQTECEalklqmaekdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRlel 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1760 SKGSLMIDEK----RRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNnetLKCGLERLNKEL 1835
Cdd:pfam15921 607 QEFKILKDKKdakiRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS---LSEDYEVLKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1836 KAKLSEQETA---LRTKLKAATAASEaKNLNLEKQLENETKERLAVQKAnrkLEKRIKELTMNIEDERRHADQYKEQIEK 1912
Cdd:pfam15921 684 RNKSEEMETTtnkLKMQLKSAQSELE-QTRNTLKSMEGSDGHAMKVAMG---MQKQITAKRGQIDALQSKIQFLEEAMTN 759
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1913 ANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKL 1966
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1025-1698 |
6.65e-11 |
|
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: 67.94 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1025 VALIEDQNHKLVKEKKLLEERANDL--SQTLAEEEEKAKHLAKLKVKHESTI-AELEERLLKDH---QQRQEADRSKRKI 1098
Cdd:pfam12128 203 VAILEDDGVVPPKSRLNRQQVEHWIrdIQAIAGIMKIRPEFTKLQQEFNTLEsAELRLSHLHFGyksDETLIASRQEERQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1099 ETEvADLKEQINERRMQIEEMQQQLvKREEELAQTLVRIDEESAAKAAAQKTQRElesqlaeiQEDLEAEKLARSKAEKQ 1178
Cdd:pfam12128 283 ETS-AELNQLLRTLDDQWKEKRDEL-NGELSAADAAVAKDRSELEALEDQHGAFL--------DADIETAAADQEQLPSW 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1179 KRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESAN---------------HESTLMDMRHKHAQEI 1243
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKireardrqlavaeddLQALESELREQLEAGK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1244 SSINEQLENLKKMKGGL----------EKSKQQLEA-----ENADLATELRNVNQSRQENDRRrkQAETQIAELQVKLAD 1308
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELklrlnqatatPELLLQLENfderiERAREEQEAANAEVERLQSELR--QARKRRDQASEALRQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1309 VDRVRVELQDKVTKLQQE-------------------SENITQQLDEAEL--------KASAAIKSAGNLESQLTEAQQL 1361
Cdd:pfam12128 511 ASRRLEERQSALDELELQlfpqagtllhflrkeapdwEQSIGKVISPELLhrtdldpeVWDGSVGGELNLYGVKLDLKRI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1362 -------LEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTnyEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKK 1434
Cdd:pfam12128 591 dvpewaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL--EKASREETFARTALKNARLDLRRLFDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1435 MNKDIETLQRQIQElqaANDRLDKSKKKIQSELEDAtieLDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAER 1514
Cdd:pfam12128 669 KNKALAERKDSANE---RLNSLEAQLKQLDKKHQAW---LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARR 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1515 EAREKETKVLSLTRELDEAFEKIDelETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAElkaQNEELEDDLQ 1594
Cdd:pfam12128 743 SGAKAELKALETWYKRDLASLGVD--PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQ---RRPRLATQLS 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1595 LTEDAKLRLEVNMQALRAQFERDIQAKEEQSeekrrglvKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMN 1674
Cdd:pfam12128 818 NIERAISELQQQLARLIADTKLRRAKLEMER--------KASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIG 889
|
730 740
....*....|....*....|....*.
gi 158285519 1675 --NKVKEDALKQAKKLQAQIKDAIRD 1698
Cdd:pfam12128 890 erLAQLEDLKLKRDYLSESVKKYVEH 915
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1240-1464 |
6.99e-11 |
|
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: 66.33 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1240 AQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQdk 1319
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1320 vTKLQQESENITQQLDEAELK--------------ASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEA 1385
Cdd:COG4942 97 -AELEAQKEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1386 LQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQ 1464
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1091-1344 |
9.63e-11 |
|
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: 65.94 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1091 ADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEesaakaaAQKTQRELESQLAEIQEDLEaekl 1170
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1171 arsKAEKQKRDLNEELEALKNELldsldttaAQQELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEissINEQL 1250
Cdd:COG4942 87 ---ELEKEIAELRAELEAQKEEL--------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA---RREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1251 ENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENI 1330
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....
gi 158285519 1331 TQQLDEAELKASAA 1344
Cdd:COG4942 233 EAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1430-1650 |
1.08e-10 |
|
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: 65.94 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1430 ESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLA----EEKAISEQV 1505
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAelekEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1506 AQERD-------AAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQ 1578
Cdd:COG4942 100 EAQKEelaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1579 LAELKAQNEELEddlqltedaklRLEVNMQALRAQFERDIQAKEEQSEEKRRGlVKALRDLEAELDEERKQR 1650
Cdd:COG4942 180 LAELEEERAALE-----------ALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1407-1761 |
1.09e-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: 67.02 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1407 LNFTIQEMKKRSEEDSDIAkELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDAtieldtQRTKVLELEK 1486
Cdd:TIGR02169 148 ISMSPVERRKIIDEIAGVA-EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------ERYQALLKEK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1487 KQKNFDKVLAEEKAISEQVAQerdaAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELA-NTQGTADKNV 1565
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEA----IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeEEQLRVKEKI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1566 HELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFErDIQAKEEQSEEKRRGLVKALRDLEAELDE 1645
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1646 ERKQ----RAAAVAAKKKLEgDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAaisKESERKVK 1721
Cdd:TIGR02169 376 VDKEfaetRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK---EDKALEIK 451
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 158285519 1722 TLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSK 1761
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
35-78 |
1.10e-10 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 58.21 E-value: 1.10e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 158285519 35 KRLVWVPHESQGFVAASIKGERGDEVEVELaETGKRVLVLKDDI 78
Cdd:pfam02736 3 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
884-1650 |
1.26e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKLeNLSKNS---QEYEKKYQQAMEEKThlaEQLQAEIELCAEAEEGRARLVARKQELEE 960
Cdd:PRK04863 315 ELAELNEAESDLEQDYQAASDHL-NLVQTAlrqQEKIERYQADLEELE---ERLEEQNEVVEEADEQQEENEARAEAAEE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 961 LMQDLES-------RIEEEEER-------VNALTSEKKKLQ---INIQDLEEQLEEEEAARQKLQLEKVQLDAKLkKMEE 1023
Cdd:PRK04863 391 EVDELKSqladyqqALDVQQTRaiqyqqaVQALERAKQLCGlpdLTADNAEDWLEEFQAKEQEATEELLSLEQKL-SVAQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1024 DVALIEDQNHKLVkeKKLLEE----RANDLSQTLAEEEEKAKHLAKLKVKHESTIAELE---------ERLLKDHQQRQ- 1089
Cdd:PRK04863 470 AAHSQFEQAYQLV--RKIAGEvsrsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEqrlrqqqraERLLAEFCKRLg 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1090 -------EADRSKRKIETEVADLKEQ---INERRMQIEEMQQQLVKREEELAQT----------LVRIDEESaakAAAQK 1149
Cdd:PRK04863 548 knlddedELEQLQEELEARLESLSESvseARERRMALRQQLEQLQARIQRLAARapawlaaqdaLARLREQS---GEEFE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1150 TQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALknelldSLDTTAAQQELRSKREQEVATLKKTLEDESANHE 1229
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLED 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1230 STLMDMRH---KHA---QEISSINEQLENLKKMKGGL---EKSKQQLeaENADLATELRNVNQSRQENDRR--------- 1291
Cdd:PRK04863 699 APYFSALYgpaRHAivvPDLSDAAEQLAGLEDCPEDLyliEGDPDSF--DDSVFSVEELEKAVVVKIADRQwrysrfpev 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1292 ----RKQAETQIAELqvkladvdrvRVELQDKVTKLQQESENI--TQQLDEA---ELKASAAIKSAGNLESQLTEAQQLL 1362
Cdd:PRK04863 777 plfgRAAREKRIEQL----------RAEREELAERYATLSFDVqkLQRLHQAfsrFIGSHLAVAFEADPEAELRQLNRRR 846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1363 EEETRQKLALSSKLRQIESEKEALqeqleedeeaktnyEKKLAELNFTIQEMKKRseEDSDIAKELEESKKKMnKDIETL 1442
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQA--------------KEGLSALNRLLPRLNLL--ADETLADRVEEIREQL-DEAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1443 QRQIQELQAANDRLDKSKKKIQSELEDatieLDTQRTKVLELEKKQKNFDK-------VLAEEKAISEQVAQERDAAERE 1515
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDPEQ----FEQLKQDYQQAQQTQRDAKQqafalteVVQRRAHFSYEDAAEMLAKNSD 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1516 AREKetkvlsLTRELDEAFEKIDELETKRKGLQNELDElaNTQGTADknvheLEKAKRALESQLAELKaqnEELED---- 1591
Cdd:PRK04863 986 LNEK------LRQRLEQAEQERTRAREQLRQAQAQLAQ--YNQVLAS-----LKSSYDAKRQMLQELK---QELQDlgvp 1049
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1592 -DLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQS--EEKRRGLVKALRDLEAELDEERKQR 1650
Cdd:PRK04863 1050 aDSGAEERARARRDELHARLSANRSRRNQLEKQLTfcEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1095-1816 |
1.55e-10 |
|
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: 66.79 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1095 KRKIETEVADLKEQINERRMQIEEMQQQLVKReeelaQTLVRIDEESAAKAAAQKTQRELESQLAEiqedLEAEKLARSK 1174
Cdd:pfam12128 199 KSMIVAILEDDGVVPPKSRLNRQQVEHWIRDI-----QAIAGIMKIRPEFTKLQQEFNTLESAELR----LSHLHFGYKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1175 AEKQKRDLNEELEALKNELLDSLDTTAAQ-QELRSKREQEVATLKKTLEdeSANHESTLMDMRHKHAQEissinEQLENL 1253
Cdd:pfam12128 270 DETLIASRQEERQETSAELNQLLRTLDDQwKEKRDELNGELSAADAAVA--KDRSELEALEDQHGAFLD-----ADIETA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1254 KKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAElqvKLADVDRVRVELQDKVTKLQQESENITQQ 1333
Cdd:pfam12128 343 AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR---DIAGIKDKLAKIREARDRQLAVAEDDLQA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1334 LdEAELKASaaiksagnLESQLTEAQqllEEETRQKLALSS-KLRQIESEKEALQeqleedeeaKTNYEKKLAELNFTIQ 1412
Cdd:pfam12128 420 L-ESELREQ--------LEAGKLEFN---EEEYRLKSRLGElKLRLNQATATPEL---------LLQLENFDERIERARE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1413 EMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQaandrldkskkKIQSELEDATIELDTQRTKVLELEKKQ---- 1488
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE-----------ERQSALDELELQLFPQAGTLLHFLRKEapdw 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1489 -KNFDKVLAEEKAISEQVAQERDAAereAREKETKVLSLTRELDEAfeKIDELETKRKGLQNELDELANTQGTADKNVHE 1567
Cdd:pfam12128 548 eQSIGKVISPELLHRTDLDPEVWDG---SVGGELNLYGVKLDLKRI--DVPEWAASEEELRERLDKAEEALQSAREKQAA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1568 LEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAEL---- 1643
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqawl 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1644 ----DEERKQRAAAVAAKKKLEGDLKDMEATL-------EMNNKVKEDALKQ--AKKLQAQIKDAIRDAEEAKAAKEELA 1710
Cdd:pfam12128 703 eeqkEQKREARTEKQAYWQVVEGALDAQLALLkaaiaarRSGAKAELKALETwyKRDLASLGVDPDVIAKLKREIRTLER 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1711 AISKESERKVKTLEADlmQLTEDLSSSERARRAAEgerdelLEEINSnsskgslmidEKRRLEARIAALEEELEEEQSNL 1790
Cdd:pfam12128 783 KIERIAVRRQEVLRYF--DWYQETWLQRRPRLATQ------LSNIER----------AISELQQQLARLIADTKLRRAKL 844
|
730 740
....*....|....*....|....*.
gi 158285519 1791 ELMVDRNRKAQLTIEQLTTELATEKS 1816
Cdd:pfam12128 845 EMERKASEKQQVRLSENLRGLRCEMS 870
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
884-1236 |
2.28e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQ 963
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 964 DLESRIEEEEERVNA-------LTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALiEDQNHKLV 1036
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1037 KEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQIN------ 1110
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerir 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1111 ERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQ-----LAEIQEDLEAEKLARSKAEKQKRDLNEE 1185
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREE 675
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 158285519 1186 LEALKNELLDSLDTTAAQQELRSKREQEVATLKK--TLEDESANHESTLMDMR 1236
Cdd:PRK02224 676 RDDLQAEIGAVENELEELEELRERREALENRVEAleALYDEAEELESMYGDLR 728
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1603-1955 |
2.38e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1603 LEVNMQALRAQFERDIQAKEEQSEEKRR---GLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKE 1679
Cdd:COG1196 198 LERQLEPLERQAEKAERYRELKEELKELeaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1680 DALKQAKKLQAQIKDairdaeeakaakeelaaiskeserkvktLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNS 1759
Cdd:COG1196 278 ELELELEEAQAEEYE----------------------------LLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1760 SKGSLMIDEKRRLEARIAALEEELeeeqsnlelmvdrnRKAQLTIEQLTTElateksnsqnnetlkcgLERLNKELKAKL 1839
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEEL--------------EEAEAELAEAEEA-----------------LLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1840 SEQETALRTKLKAATAASEAKN--LNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRM 1917
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAqlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
330 340 350
....*....|....*....|....*....|....*...
gi 158285519 1918 KTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEAL 1955
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1170-1740 |
2.38e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1170 LARSKAEKQKRDLNE----------ELEALKNELLDSLDT-TAAQQELRSKREQevatlKKTLEDESANHEstlmdmRHK 1238
Cdd:COG4913 197 LHKTQSFKPIGDLDDfvreymleepDTFEAADALVEHFDDlERAHEALEDAREQ-----IELLEPIRELAE------RYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1239 HAQEISSINEQLENLKKMKGGlEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVElqd 1318
Cdd:COG4913 266 AARERLAELEYLRAALRLWFA-QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE--- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1319 kvtKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEetrQKLALSSKLRQIESEKEALQEQLEEDEEAKT 1398
Cdd:COG4913 342 ---QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---LRAEAAALLEALEEELEALEEALAEAEAALR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1399 NYEKKLAELNFTIQEMKKRseeDSDIAKELEESKKKMNKDietLQRQIQELQAANDRLDKSKKkiQSELEDAtIE--LDT 1476
Cdd:COG4913 416 DLRRELRELEAEIASLERR---KSNIPARLLALRDALAEA---LGLDEAELPFVGELIEVRPE--EERWRGA-IErvLGG 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1477 QRTKVLeleKKQKNFDKVLA-------EEKAISEQVAQERDAAEREAREKET---KVLS--------LTRELDEAF---- 1534
Cdd:COG4913 487 FALTLL---VPPEHYAAALRwvnrlhlRGRLVYERVRTGLPDPERPRLDPDSlagKLDFkphpfrawLEAELGRRFdyvc 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1535 -EKIDELETKRKGL-----------------QNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLT 1596
Cdd:COG4913 564 vDSPEELRRHPRAItragqvkgngtrhekddRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1597 EDAKLRLevnmQALRAQFERDI-----QAKEEQSEEKRRGLVKALRDLEaELDEERKQRAAAVAAKKKLEGDLKDMEATL 1671
Cdd:COG4913 644 QERREAL----QRLAEYSWDEIdvasaEREIAELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRL 718
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1672 EMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKV-KTLEADLMQLTEDLSSSERA 1740
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEE 788
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1338-1929 |
3.39e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1338 ELKASAAIKSAGNLESQLTEAQQLLEEetrqklaLSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELnftiqemkkr 1417
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAE-------LDEEIERYEEQREQARETRDEADEVLEEHEERREEL---------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1418 SEEDSDIAkELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKI--QSELEDATIELDTQRTKvlELEKKQKNFDKVL 1495
Cdd:PRK02224 254 ETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARRE--ELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1496 AEE----KAISEQVAQERDAA---EREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHEL 1568
Cdd:PRK02224 331 EECrvaaQAHNEEAESLREDAddlEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1569 EKAKRALESQLAELKAQNEELEDDLQLTEDaklRLEVNMQALRAQferdiQAKEEQSEEKRRGLVKALRDLEAELDEerk 1648
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARE---RVEEAEALLEAG-----KCPECGQPVEGSPHVETIEEDRERVEE--- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1649 qraaavaakkkLEGDLKDMEATLEMNNKvKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLM 1728
Cdd:PRK02224 480 -----------LEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1729 QLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEaRIAALEEELEEEQSNLELMvdRNRKAQLTieqlt 1808
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERL--REKREALA----- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1809 telateKSNSQNNETLKCGLERlNKELKAKLSEQE-TALRTKLKAATAASEaknlNLEKQLENETKERLAVQKANRKLEK 1887
Cdd:PRK02224 620 ------ELNDERRERLAEKRER-KRELEAEFDEARiEEAREDKERAEEYLE----QVEEKLDELREERDDLQAEIGAVEN 688
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 158285519 1888 RIKELtmniederrhaDQYKEQIEKANNRMKTLKRNLDEAEE 1929
Cdd:PRK02224 689 ELEEL-----------EELRERREALENRVEALEALYDEAEE 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1295-1525 |
4.04e-10 |
|
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: 64.01 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1295 AETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSs 1374
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1375 klRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAAND 1454
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1455 RLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLS 1525
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1317-1536 |
8.06e-10 |
|
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: 62.86 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1317 QDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEA 1396
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1397 KTNYEKKLAELNFTIQEMKKRSEED----SDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATI 1472
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1473 ELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEK 1536
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1148-1385 |
9.04e-10 |
|
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: 62.86 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1148 QKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELldsldtTAAQQELRskreqevatlkkTLEDESAN 1227
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI------AALARRIR------------ALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1228 HESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAE----NADLATELRNVNQSRQENDRRRKQAEtqiaELQ 1303
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAE----ELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1304 VKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEK 1383
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
..
gi 158285519 1384 EA 1385
Cdd:COG4942 237 AA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1411-1934 |
1.73e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1411 IQEMKKRSEEDSDIAKELEESKKKMnkDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKN 1490
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1491 FDkvlAEEKaisEQVAQERDAAEREAREKETKVlsltRELDEAFEKID-ELETKRKGLQNELDELANTQGTADKNVHELE 1569
Cdd:COG4913 335 NG---GDRL---EQLEREIERLERELEERERRR----ARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1570 KAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQ------------SEEKRRG------ 1631
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrpEEERWRGaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1632 -------LV------KALR-----DLEAELDEERKQRAAAVAAKKKLEGD-------LKDMEATLEMNNKVK-------- 1678
Cdd:COG4913 485 ggfaltlLVppehyaAALRwvnrlHLRGRLVYERVRTGLPDPERPRLDPDslagkldFKPHPFRAWLEAELGrrfdyvcv 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1679 --EDALKQAKK---LQAQIKD-----AIRDAEEAKAAKEelaaISKESERKVKTLEADLMQLTEDLSSSERARRAAEGER 1748
Cdd:COG4913 565 dsPEELRRHPRaitRAGQVKGngtrhEKDDRRRIRSRYV----LGFDNRAKLAALEAELAELEEELAEAEERLEALEAEL 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1749 DELleeinsnsskgslmiDEKRRLEARIAALEEELeeeqsnlelmvDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGL 1828
Cdd:COG4913 641 DAL---------------QERREALQRLAEYSWDE-----------IDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1829 ERLNKELKAKLSEQETALRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELtMNIEDERRHADQYKE 1908
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA-LGDAVERELRENLEE 773
|
570 580
....*....|....*....|....*.
gi 158285519 1909 QIEKANNRMKTLKRNLDEAEEEIQKE 1934
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1428-1967 |
3.00e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1428 LEEskKKMNKDIETLQRQIQELQAANDRLDKSKKKIQ--SELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAisEQV 1505
Cdd:COG4913 218 LEE--PDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL--ELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1506 AQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQ-NELDELANTQGTADKNVHELEKAKRALESQLAELKA 1584
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1585 QNEELEDDLQltedaklrlevNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDL 1664
Cdd:COG4913 374 PLPASAEEFA-----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1665 KDMEATLEMNNKVKEDALK------QAKKLQAQIKDAIrdaeeakaakeelaaiskesERKVKTL----------EADLM 1728
Cdd:COG4913 443 LALRDALAEALGLDEAELPfvgeliEVRPEEERWRGAI--------------------ERVLGGFaltllvppehYAAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1729 QLTEDLSSSERAR--RAAEGERDELLEEINSNSSKGSLMIDE---KRRLEARIAALEEELEeeqsnlelmVD------RN 1797
Cdd:COG4913 503 RWVNRLHLRGRLVyeRVRTGLPDPERPRLDPDSLAGKLDFKPhpfRAWLEAELGRRFDYVC---------VDspeelrRH 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1798 RKAqLTIEQLTtelateksnSQNNETLKCGLERL----------NKELKAKLSEQETALRTKLKAATAASEAknlnLEKQ 1867
Cdd:COG4913 574 PRA-ITRAGQV---------KGNGTRHEKDDRRRirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEA----LEAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1868 LENETKERLAVQKANRKLEKRIKelTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECED 1947
Cdd:COG4913 640 LDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGR 717
|
570 580
....*....|....*....|
gi 158285519 1948 MLESHEALSREVNALKSKLS 1967
Cdd:COG4913 718 LEKELEQAEEELDELQDRLE 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1248-1756 |
3.05e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1248 EQLENLKKMKGGLEKSKQQLEAenadLaTELRNVNQSRQENDRRRKQAETQIAELQVKLAdvdrvrvelQDKVTKLQQES 1327
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIEL----L-EPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1328 ENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLAlssklrQIESEKEALQEQLEEDEEAKTNYEKKLAEL 1407
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE------QLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1408 NFTIqemkkrseedSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDtqrtkvlELEKK 1487
Cdd:COG4913 372 GLPL----------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-------SLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1488 QKNFD-------KVLAEEKAISE----------QVAQE----RDAAER-----------------------EAREKETKV 1523
Cdd:COG4913 435 KSNIParllalrDALAEALGLDEaelpfvgeliEVRPEeerwRGAIERvlggfaltllvppehyaaalrwvNRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1524 ------LSLTRELDEAFEK---IDELETKRKGLQNELDELANTQGTADK--NVHELEKAKRAL----------------- 1575
Cdd:COG4913 515 vyervrTGLPDPERPRLDPdslAGKLDFKPHPFRAWLEAELGRRFDYVCvdSPEELRRHPRAItragqvkgngtrhekdd 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1576 --------------ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKR-RGLVKALRDLE 1640
Cdd:COG4913 595 rrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1641 AELDEERKqraaAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERkv 1720
Cdd:COG4913 675 AELERLDA----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-- 748
|
570 580 590
....*....|....*....|....*....|....*.
gi 158285519 1721 KTLEADLMQLTEDlSSSERARRAAEGERDELLEEIN 1756
Cdd:COG4913 749 ALLEERFAAALGD-AVERELRENLEERIDALRARLN 783
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1396-1970 |
3.29e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 62.30 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1396 AKTNYEKKLAE--LNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIE 1473
Cdd:pfam02463 170 KKKEALKKLIEetENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1474 LDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQErdaaEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDE 1553
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ----EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1554 LANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRRGLV 1633
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1634 KALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAIS 1713
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1714 KESERKVKTLEADLMQLTEDLSSSERAR-RAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLEL 1792
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLaLIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1793 MVDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGLER-LNKELKAKLSEQETALRTKLKAATAASEAKNLNLEKQLENE 1871
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILnLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1872 TKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLES 1951
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570
....*....|....*....
gi 158285519 1952 HEALSREVNALKSKLSIHK 1970
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQK 744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1411-1626 |
3.50e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1411 IQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKN 1490
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1491 FDKVLAEEKAI--SEQVAqerDAAEReareketkVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHEL 1568
Cdd:COG3883 98 SGGSVSYLDVLlgSESFS---DFLDR--------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 1569 EKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSE 1626
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1137-1360 |
4.00e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1137 IDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELldsldtTAAQQELRSKREQevat 1216
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI------AEAEAEIEERREE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1217 LKKTLED-----ESANHESTLMDmrhkhAQEISSINEQLENLKKMKG-------GLEKSKQQLEAENADLATELRNVNQS 1284
Cdd:COG3883 88 LGERARAlyrsgGSVSYLDVLLG-----SESFSDFLDRLSALSKIADadadlleELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1285 RQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQ 1360
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
865-1363 |
4.67e-09 |
|
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: 61.57 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 865 LKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELRQIRDKLE-NLSKNSQEY----------EKKYQQAMEEKTHLAEQ 933
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKdNIEKKQQEInektteisntQTQLNQLKDEQNKIKKQ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 934 LQAEIELCAEAEEGRARLVARKQEL------------EELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEE 1001
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLkseisdlnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1002 AARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHL-AKLKVKhestiaELEER 1080
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKdEQIKKL------QQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1081 LLKDHQQRQEADRSKRKieTEVADLKEQINERRMQIEEMQQqlvKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAE 1160
Cdd:TIGR04523 423 LLEKEIERLKETIIKNN--SEIKDLTNQDSVKELIIKNLDN---TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1161 IqedleaeklarSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHESTLMDmrhkha 1240
Cdd:TIGR04523 498 L-----------KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE------ 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1241 QEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKV 1320
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 158285519 1321 TKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLE 1363
Cdd:TIGR04523 641 NKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMK 683
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1064-1342 |
7.31e-09 |
|
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: 60.16 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1064 AKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTlvrideesaa 1143
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1144 kaaaQKTQRELESQLAEIQEDleaekLARSKAEKQKRDLNEELEALKN--ELLDSLDTTAAQQELRSKREQEVATLKKTL 1221
Cdd:COG4942 89 ----EKEIAELRAELEAQKEE-----LAELLRALYRLGRQPPLALLLSpeDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1222 EDesanhestlmdmrhkhaqeissineqlenLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAE 1301
Cdd:COG4942 160 AE-----------------------------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 158285519 1302 LQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKAS 1342
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1528-1849 |
7.91e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1528 RELDEAFEKIDELETKRKGLQNELDELANTQGTADK-----------NVHELEKAKRALESQLAELKAQNEELEDDLQlt 1596
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqallkekreyEGYELLKEKEALERQKEAIERQLASLEEELE-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1597 edaklrlevnmqalraQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQraaAVAAKKKLEGDLKDMEATLEMNNK 1676
Cdd:TIGR02169 255 ----------------KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR---VKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1677 VKEDALKQAKKLQAQI-------KDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERD 1749
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIdkllaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1750 ELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEK----SNSQNNETLK 1825
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLK 475
|
330 340
....*....|....*....|....
gi 158285519 1826 CGLERLNKELKAKLSEQETALRTK 1849
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQA 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
953-1169 |
8.41e-09 |
|
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: 59.78 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 953 ARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQn 1032
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1033 hkLVKEKKLLEERANDLSQTLAEEE-------EKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADL 1105
Cdd:COG4942 99 --LEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1106 KEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEK 1169
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
882-1113 |
1.00e-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: 59.39 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 882 LLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEEL 961
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 962 MQDLESRIEEEEERVNALTsekKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKL 1041
Cdd:COG4942 92 IAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1042 LEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERR 1113
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1030-1487 |
1.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1030 DQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHEStiAELEERLLKDHQQRQEADRSKRKIETEVADLKEQI 1109
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1110 NE---RRMQIEEMQQQLVKREEELAQTLVRIDEEsaakaaAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEEL 1186
Cdd:COG4717 149 EEleeRLEELRELEEELEELEAELAELQEELEEL------LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1187 EALKNELLDSLDTTAAQQELRSKREQEVATLKktledesanhESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQ 1266
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLI----------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1267 LEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAik 1346
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ-- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1347 sagNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAElnftiqemKKRSEEDSDIAK 1426
Cdd:COG4717 371 ---EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--------EELEEELEELEE 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1427 ELEESKKKmnkdIETLQRQIQELQAANDRLDKSKkkiqsELEDATIELDTQRTKVLELEKK 1487
Cdd:COG4717 440 ELEELEEE----LEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1587-1943 |
1.26e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1587 EELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEK---RRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGD 1663
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELReleLALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1664 LKDMEATLEmnnkVKEDALKQAKKLQAQIKDAIrdaeeakaakeelaaisKESERKVKTLEADLMQLTEDLSSSERARRA 1743
Cdd:TIGR02168 262 LQELEEKLE----ELRLEVSELEEEIEELQKEL-----------------YALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1744 AEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELA--TEKSNSQNN 1821
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1822 E--TLKCGLERLNKELKAKLSEQETALRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELtmniede 1899
Cdd:TIGR02168 401 EieRLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA------- 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 158285519 1900 RRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQR 1943
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1511-1698 |
2.04e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1511 AAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELE 1590
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1591 DDLQLTEDAKLRLEVNMQAL-------------------------------RAQFERDIQAKEEQSEEKRRGLVKALRDL 1639
Cdd:COG4942 97 AELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1640 EAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRD 1698
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1315-1943 |
2.95e-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: 59.21 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1315 ELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQlLEEETRQKLALSSKLRQIESEKEALQEQLEEDE 1394
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ-QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1395 EAKTNYEKKLAELNFTIQ----------EMKKRSEEDSDIAKELEESKKKMNK----------------DIETLQRQIQE 1448
Cdd:TIGR00618 270 EELRAQEAVLEETQERINrarkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSrakllmkraahvkqqsSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1449 LQAANDRLDKSK--------------------KKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQE 1508
Cdd:TIGR00618 350 LHSQEIHIRDAHevatsireiscqqhtltqhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1509 RDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQgtadkNVHELEKAKRALESQLAELKAQNEE 1588
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE-----QIHLQETRKKAVVLARLLELQEEPC 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1589 LEDDLQLTEDAKLRLEVNMQALraqferdiQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLkdmE 1668
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPGPL--------TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF---S 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1669 ATLEMNNKVKEDalkqAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSER---ARRAAE 1745
Cdd:TIGR00618 574 ILTQCDNRSKED----IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQElalKLTALH 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1746 GERDELLEEINSNSSKgSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEK---SNSQNNE 1822
Cdd:TIGR00618 650 ALQLTLTQERVREHAL-SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRefnEIENASS 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1823 TLKCGLERLNKELKAKLSEQETALRTKLKAATAASEAKNL-------------NLEKQLENETKERLAVQKANRKLEKRI 1889
Cdd:TIGR00618 729 SLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEevtaalqtgaelsHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1890 K------ELTMNIEDERRHAD--QYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQR 1943
Cdd:TIGR00618 809 GqeipsdEDILNLQCETLVQEeeQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1294-1520 |
3.56e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1294 QAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEetrQKLALS 1373
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1374 SKLRQIeSEKEALQEQLEEDEEAKTnyekkLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAAN 1453
Cdd:COG3883 90 ERARAL-YRSGGSVSYLDVLLGSES-----FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1454 DRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKE 1520
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1003-1470 |
3.62e-08 |
|
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: 58.60 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1003 ARQKLQLEKVQLDAKLKKMEEDVALIE----------------DQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAK- 1065
Cdd:pfam05557 5 IESKARLSQLQNEKKQMELEHKRARIElekkasalkrqldresDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1066 -------------LKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQ----------INERRMQIEEMQQQ 1122
Cdd:pfam05557 85 lealnkklnekesQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERldllkakaseAEQLRQNLEKQQSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1123 LVKREEELAQTLVRIDEESAAKAAAQKTQRELESqLAEIQEDLEAEKLARSKAEKQKRD---LNEELEALKNELL---DS 1196
Cdd:pfam05557 165 LAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR-IPELEKELERLREHNKHLNENIENkllLKEEVEDLKRKLEreeKY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1197 LDTTAAQQELRSKREQEVATLKKTLEDESANHESTlMDMRhkhaQEISSINEQLENLKKMKGGLEKSKQQLEAENADLAT 1276
Cdd:pfam05557 244 REEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP-EDLS----RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1277 ELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVR------VELQDKVTKLQQESENITQQLDEAELKASAAIKSAGN 1350
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgyraiLESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1351 LESQLTeaqQLLEEETRQKLALSSKLRQIESEKE-ALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEE--------- 1420
Cdd:pfam05557 399 MEAQLS---VAEEELGGYKQQAQTLERELQALRQqESLADPSYSKEEVDSLRRKLETLELERQRLREQKNElemelerrc 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 1421 ---DSDIA--KELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDA 1470
Cdd:pfam05557 476 lqgDYDPKktKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQV 530
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
888-1286 |
4.00e-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: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 888 QEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAeegrarlvarkqeleelmqdLES 967
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKA--------------------LAE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 968 RIEEEEERVNALTSEKKKLQINIQDLEEQLEeeeaaRQKLQLeKVQLDAKLKKMEEDvalIEDQNHKLVKEKklLEERAN 1047
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQLDKKHQAWLEEQK-----EQKREA-RTEKQAYWQVVEGA---LDAQLALLKAAI--AARRSG 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1048 DLSQTLAEEEEKAKHLAKLKVKhestiaelEERLLKDHQQRQEADRSkrkietevadlKEQINERRMQIEE----MQQQL 1123
Cdd:pfam12128 745 AKAELKALETWYKRDLASLGVD--------PDVIAKLKREIRTLERK-----------IERIAVRRQEVLRyfdwYQETW 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1124 VKREEELAQTLVRIDEEsaakaaaqktQRELESQLAEIQEDLeaeKLARSKAEKQkRDLNEELEALKNELLDSLDTtaaq 1203
Cdd:pfam12128 806 LQRRPRLATQLSNIERA----------ISELQQQLARLIADT---KLRRAKLEME-RKASEKQQVRLSENLRGLRC---- 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1204 qelrskREQEVATLKKTLEDESANHEST-----LMDMRHKHAQEISSINEQLENLK-----KMKGGLEKSKQQLEAENAD 1273
Cdd:pfam12128 868 ------EMSKLATLKEDANSEQAQGSIGerlaqLEDLKLKRDYLSESVKKYVEHFKnviadHSGSGLAETWESLREEDHY 941
|
410
....*....|...
gi 158285519 1274 LATELRNVNQSRQ 1286
Cdd:pfam12128 942 QNDKGIRLLDYRK 954
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1038-1908 |
4.46e-08 |
|
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: 58.81 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1038 EKKLLEERANDLSQTLAEEEEKakhLAKLKVKHESTIAELE-----ERLLK-------DHQQR-QEADRSKRKIE---TE 1101
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ---LAEEQYRLVEMARELEelsarESDLEqdyqaasDHLNLvQTALRQQEKIEryqED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1102 VADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEesaakaaaqktqreLESQLAEIQEDLEAEKlARSKAEKQKRD 1181
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS--------------LKSQLADYQQALDVQQ-TRAIQYQQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1182 LNEELEALKNelLDSLDTTAA---QQELRSKREQ---EVATLKKTLEDESANHEstlmdmRHKHAqeissineqLENLKK 1255
Cdd:COG3096 421 ALEKARALCG--LPDLTPENAedyLAAFRAKEQQateEVLELEQKLSVADAARR------QFEKA---------YELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1256 MKGGLEKSK-----QQLEAENADLATELRNVNQSRQE------NDRRRKQAETQIAELQVKLAdvdrVRVELQDKVTKLQ 1324
Cdd:COG3096 484 IAGEVERSQawqtaRELLRRYRSQQALAQRLQQLRAQlaeleqRLRQQQNAERLLEEFCQRIG----QQLDAAEELEELL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1325 QESEnitQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQK---LALSSKLRQIESEKEALQEQLEedeeAKTNYE 1401
Cdd:COG3096 560 AELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQ----EVTAAM 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1402 KKLAElnftiQEMKKRSEEDsdiakELEESKkkmnkdiETLQRQIQELQAAND----RLDKSKKKIQSEL-----EDATI 1472
Cdd:COG3096 633 QQLLE-----REREATVERD-----ELAARK-------QALESQIERLSQPGGaedpRLLALAERLGGVLlseiyDDVTL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1473 E--------------------LDTQRTKVLELEKkqknfdkvLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDE 1532
Cdd:COG3096 696 EdapyfsalygparhaivvpdLSAVKEQLAGLED--------CPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQW 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1533 AFEKIDEL--------ETKRKGLQNELDELANTQGTADKNVHELEKAKRAL----------------ESQLAELKAQNEE 1588
Cdd:COG3096 768 RYSRFPEVplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFsqfvgghlavafapdpEAELAALRQRRSE 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1589 LEDDLQltedaklRLEVNMQALRAQFErdiQAKEEQSEEKR----------RGLVKALRDLEAELDEERKQRAAAVAAKK 1658
Cdd:COG3096 848 LERELA-------QHRAQEQQLRQQLD---QLKEQLQLLNKllpqanlladETLADRLEELREELDAAQEAQAFIQQHGK 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1659 KLEgDLKDMEATLEmNNKVKEDALK----QAKKLQAQIKdairdaeeakaakeelaaiskeseRKVKTLEaDLMQLTEDL 1734
Cdd:COG3096 918 ALA-QLEPLVAVLQ-SDPEQFEQLQadylQAKEQQRRLK------------------------QQIFALS-EVVQRRPHF 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1735 SSSERARRAAEGErdELLEEInsnssKGSLMIDEKRRLEARIAAleeeleeeqsnlelmvdrnRKAQLTIEQLTTELATE 1814
Cdd:COG3096 971 SYEDAVGLLGENS--DLNEKL-----RARLEQAEEARREAREQL-------------------RQAQAQYSQYNQVLASL 1024
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1815 KSNSQN-NETLKCGLERLNK-ELKAKLSEQETAL--RTKLKAATAASEAKNLNLEKQlenetkerLAVQKANRK-LEKRI 1889
Cdd:COG3096 1025 KSSRDAkQQTLQELEQELEElGVQADAEAEERARirRDELHEELSQNRSRRSQLEKQ--------LTRCEAEMDsLQKRL 1096
|
970
....*....|....*....
gi 158285519 1890 KELTMNIEDERRHADQYKE 1908
Cdd:COG3096 1097 RKAERDYKQEREQVVQAKA 1115
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
896-1506 |
5.01e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 896 EDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIElcaeaeegraRLVARKQELEELMqdlesrieeeeer 975
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMD----------DYNNLKSALNELS------------- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 976 vnALTSEKKKLQINIQDleeqleeeeaARQKLQLEKVQLDaKLKKMEEDVALIEdqNHKLVKEKKLLEERANDLSQtLAE 1055
Cdd:PRK01156 246 --SLEDMKNRYESEIKT----------AESDLSMELEKNN-YYKELEERHMKII--NDPVYKNRNYINDYFKYKND-IEN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1056 EEEKAKHLAKLKVKHESTIAELEErLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLV 1135
Cdd:PRK01156 310 KKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIER 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1136 RIDEESAAKAAAQKTQRELESQLAEIQEDLEaeklarsKAEKQKRDLNEELEALKnELLDSLDTTAAQQELRSKreqeVA 1215
Cdd:PRK01156 389 MSAFISEILKIQEIDPDAIKKELNEINVKLQ-------DISSKVSSLNQRIRALR-ENLDELSRNMEMLNGQSV----CP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1216 TLKKTLEDESANHestlmdMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATElrNVNQSRQEnDRRRKQA 1295
Cdd:PRK01156 457 VCGTTLGEEKSNH------IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE--EINKSINE-YNKIESA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1296 ETQIAELQVKLAdvdrvrvELQDKVTKLQQESENI-TQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLA-LS 1373
Cdd:PRK01156 528 RADLEDIKIKIN-------ELKDKHDKYEEIKNRYkSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNdLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1374 SKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAAN 1453
Cdd:PRK01156 601 SRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIE 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 1454 DRLDKSKKKIQSELED-----ATIEldTQRTKVLELEKKQKNFDKVLAEEKAISEQVA 1506
Cdd:PRK01156 681 DNLKKSRKALDDAKANrarleSTIE--ILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
902-1443 |
5.10e-08 |
|
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: 58.21 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 902 IRDKLENLSKNSQ-EYEKKYQQAMEEKTHLAEQLQAEIE-LCAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNAL 979
Cdd:pfam15921 243 VEDQLEALKSESQnKIELLLQQHQDRIEQLISEHEVEITgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 980 TSEKKKLQINIQDLEEQLEEEEAARQKlQL-----EKVQLDAKLKKMEEDVALIEDQNHKLVKEkklLEERANDLSQtla 1054
Cdd:pfam15921 323 ESTVSQLRSELREAKRMYEDKIEELEK-QLvlansELTEARTERDQFSQESGNLDDQLQKLLAD---LHKREKELSL--- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1055 eEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQ-------INERRMQIEEMQQQLVKRE 1127
Cdd:pfam15921 396 -EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERqmaaiqgKNESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1128 EELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAeKQKRDLN-EELEALKNELLDSLDTTAAQQEL 1206
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL-RSRVDLKlQELQHLKNEGDHLRNVQTECEAL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1207 R---SKREQEVATLKKTLEDES---ANHESTLMDMRHKHAQEISSINE---QLENLKKMKGGLEKSKQQLEAENADLATE 1277
Cdd:pfam15921 554 KlqmAEKDKVIEILRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEINDrrlELQEFKILKDKKDAKIRELEARVSDLELE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1278 -----------LRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAE-------- 1338
Cdd:pfam15921 634 kvklvnagserLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQseleqtrn 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1339 -LKA-----SAAIKSAGNLESQLTEAQ----------QLLEEET-----------RQKLALSSKLRQIESEKEALQEQLE 1391
Cdd:pfam15921 714 tLKSmegsdGHAMKVAMGMQKQITAKRgqidalqskiQFLEEAMtnankekhflkEEKNKLSQELSTVATEKNKMAGELE 793
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1392 EDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEES----KKKMNKDIETLQ 1443
Cdd:pfam15921 794 VLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvrlKLQHTLDVKELQ 849
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1397-1963 |
6.90e-08 |
|
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: 57.72 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1397 KTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDT 1476
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1477 QRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKvlslTRELDEAFEKIDELETKRKGLQNELDELAN 1556
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK----TTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1557 TQGTADKNVHELEKAKRALESQLAELKAQNEeleddlqltedaklrlevnmQALRAQFERDIQAKEEQseekrrglvkaL 1636
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKE--------------------QDWNKELKSELKNQEKK-----------L 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1637 RDLEAELDEERKQRAAAVAAKKKLEGDLKDmeatLEMNNKVKEDALKQAKKlqaQIKDAIRDAEEAKAAKEELAAISKES 1716
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTN----SESENSEKQRELEEKQN---EIEKLKKENQSYKQEIKNLESQINDL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1717 ERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDR 1796
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1797 NRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQETA--------LRTKLKAATAASEAKNLNLEKQL 1868
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKieklesekKEKESKISDLEDELNKDDFELKK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1869 ENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDM 1948
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
570
....*....|....*
gi 158285519 1949 LESHEALSREVNALK 1963
Cdd:TIGR04523 637 KSKKNKLKQEVKQIK 651
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1445-1967 |
7.36e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1445 QIQELQAANDRLDKSKKKIQSELEDatIELDTQRTKVLE--LEKKQKNFDKVLAEEKAISEQvaqerdaaEREAREKETK 1522
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIER--LEKFIKRTENIEelIKEKEKELEEVLREINEISSE--------LPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1523 VLSLTRELDEAFEKIDELETKRKGLQneldelantqgtadKNVHELEKAKRALESQLAELKAQNEELEDDL----QLTED 1598
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLE--------------GSKRKLEEKIRELEERIEELKKEIEELEEKVkelkELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1599 AKLRLEVNmqALRAQF---ERDIQAKEEQSEEKRRGLVKALRDLE---AELDEERKQRAAAVAAKKKLEGDLKdmeaTLE 1672
Cdd:PRK03918 292 AEEYIKLS--EFYEEYldeLREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHE----LYE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1673 MNNKVKEDALKQAKKLQAQIKDAIRDAEeakaakeelaaisKESERKVKTLEADLMQLTEDLSSSERARraaeGERDELL 1752
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-------------EELEKAKEEIEEEISKITARIGELKKEI----KELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1753 EEINSNSSKGSL---MIDEKRRLEArIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNET---LKC 1826
Cdd:PRK03918 429 EELKKAKGKCPVcgrELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeqLKE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1827 GLERLNKELKAKLSEQETALR-TKLKAATAASEAKNLNLEKQLENETKERLA--------VQKANRKLEKRIKELTMNIE 1897
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEYEkLKEKLIKLKGEIKSLKKELEKLEELKKKLAelekkldeLEEELAELLKELEELGFESV 587
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1898 DERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKLS 1967
Cdd:PRK03918 588 EELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
986-1448 |
8.62e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.50 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 986 LQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDValiEDQNHKLVKEKKL--LEERANDLSQTLAEEEEKAKHL 1063
Cdd:PRK10246 431 LHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRY---KEKTQQLADVKTIceQEARIKDLEAQRAQLQAGQPCP 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1064 AKLKVKHEStIAELEERLLKDHQQRQEAdrskrkIETEVADLKEQINERRMQIEEMQQQLvKREEELAQTLVRidEESAA 1143
Cdd:PRK10246 508 LCGSTSHPA-VEAYQALEPGVNQSRLDA------LEKEVKKLGEEGAALRGQLDALTKQL-QRDESEAQSLRQ--EEQAL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1144 KAAAQKTQRELESQLAeIQEDLEAEKLARSKAEKQKRDLNEELEaLKNELldsldttAAQQELRSKREQEVATLKKTLED 1223
Cdd:PRK10246 578 TQQWQAVCASLNITLQ-PQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQI-------AAHNQQIIQYQQQIEQRQQQLLT 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1224 E---------SANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQendrrrkQ 1294
Cdd:PRK10246 649 AlagyaltlpQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWR-------Q 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1295 AETQIAELQVKLAdvdrvrvELQDKVTKLQQESENITQQLDEAeLKASAAIKSAGNLE--------SQLTEAQQLLEEET 1366
Cdd:PRK10246 722 VHEQCLSLHSQLQ-------TLQQQDVLEAQRLQKAQAQFDTA-LQASVFDDQQAFLAalldeetlTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1367 RQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMnkdiETLQRQI 1446
Cdd:PRK10246 794 QQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQ----QALMQQI 869
|
..
gi 158285519 1447 QE 1448
Cdd:PRK10246 870 AQ 871
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1086-1345 |
1.18e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1086 QQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQ--LVKREEELAQTLVRIDEesaakaaaqktqreLESQLAEIQE 1163
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSE--------------LESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1164 DL-EAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQElrskreQEVATLKKTLEDESanhestlmdmrhkhaQE 1242
Cdd:COG3206 234 ELaEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNH---------------PD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1243 ISSINEQLENLKkmkgglekskQQLEAENADLATELRNvnqSRQENDRRRKQAETQIAELQVKLADVDRVRVE---LQDK 1319
Cdd:COG3206 293 VIALRAQIAALR----------AQLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAElrrLERE 359
|
250 260
....*....|....*....|....*.
gi 158285519 1320 VTKLQQESENITQQLDEAELKASAAI 1345
Cdd:COG3206 360 VEVARELYESLLQRLEEARLAEALTV 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1401-1594 |
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: 55.54 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1401 EKKLAELNFTIQEMKKR----SEEDSDIAKELEESKKKM----------NKDIETLQRQIQELQAANDRLDKSKKKIQSE 1466
Cdd:COG4942 26 EAELEQLQQEIAELEKElaalKKEEKALLKQLAALERRIaalarriralEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1467 LEDATIELDTQ-RTKVLELEKKQKNFDKVLAEEKAIsEQVAQERDAAEREAREKETKVLSLTRELDeafEKIDELETKRK 1545
Cdd:COG4942 106 LAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYL-KYLAPARREQAEELRADLAELAALRAELE---AERAELEALLA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 158285519 1546 GLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQ 1594
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1053-1221 |
2.01e-07 |
|
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: 54.16 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1053 LAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEmqqqlVKREEELAQ 1132
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1133 TLVRIDeesaakaAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSL-DTTAAQQELRSKRE 1211
Cdd:COG1579 94 LQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELaELEAELEELEAERE 166
|
170
....*....|
gi 158285519 1212 QEVATLKKTL 1221
Cdd:COG1579 167 ELAAKIPPEL 176
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
954-1272 |
2.26e-07 |
|
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: 55.90 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 954 RKQELEELMQDLESRIEEEEERVNALTSEKKKL----------QINIQDLEEQLEEEEAARQKLQLEKVQLDAKL---KK 1020
Cdd:pfam17380 238 RRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFlnqllhivqhQKAVSERQQQEKFEKMEQERLRQEKEEKAREVerrRK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1021 MEED----VALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHlaklKVKHESTIAELE-----ERLLKDHQQRQEA 1091
Cdd:pfam17380 318 LEEAekarQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE----RIRQEEIAMEISrmrelERLQMERQQKNER 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1092 DRS------KRKIETEVADLKEQINERRM------QIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLA 1159
Cdd:pfam17380 394 VRQeleaarKVKILEEERQRKIQQQKVEMeqiraeQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1160 EIQEDLEAEKLARSKAEKQKRD-LNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHESTLMDMRHK 1238
Cdd:pfam17380 474 RKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRR 553
|
330 340 350
....*....|....*....|....*....|....
gi 158285519 1239 HAQEISSINEQLENLKKMKGGLEKSKQQLEAENA 1272
Cdd:pfam17380 554 IQEQMRKATEERSRLEAMEREREMMRQIVESEKA 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
932-1132 |
2.86e-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: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 932 EQLQAEIelcAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEK 1011
Cdd:COG4942 30 EQLQQEI---AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1012 VQLDAKLKKME-----------EDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEER 1080
Cdd:COG4942 107 AELLRALYRLGrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1081 LLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQ 1132
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1250-1645 |
3.12e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1250 LENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESEN 1329
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1330 --ITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEED-EEAKTNYEKKLAE 1406
Cdd:COG4717 128 lpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1407 LNFTIQEMKKRSEEDSDIAKELEESKKKMNkdIETLQRQIQELQ-----------------AANDRLDKSKKKIQSELED 1469
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARlllliaaallallglggSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1470 ATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQN 1549
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1550 ELDELANTQGTADKNVHELEKAKRALE--SQLAELKAQNEELEDDLQLTEDAKLRL--EVNMQALRAQFERdIQAKEEQS 1625
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEE-LEEELEEL 444
|
410 420
....*....|....*....|
gi 158285519 1626 EEKRRGLVKALRDLEAELDE 1645
Cdd:COG4717 445 EEELEELREELAELEAELEQ 464
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1339-1563 |
3.96e-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: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1339 LKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRS 1418
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1419 EEdsdIAKELEESKKKMNKDIETLQRQ-----IQELQAAND--RLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNF 1491
Cdd:COG4942 93 AE---LRAELEAQKEELAELLRALYRLgrqppLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1492 DKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADK 1563
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1418-1694 |
4.19e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1418 SEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLdkskKKIQSELEDATIELDTQRTKVLELEKKQKNFDKV--- 1494
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAE----SDLEQDYQAASDHLNLVQTALRQQEKIERYQADLeel 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1495 ---LAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKA 1571
Cdd:PRK04863 361 eerLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1572 KRALESQLAELKAQNEE---LEDDLQLTEDAKLRLEVNMQAL--------RAQFERDIQAKEEQSEEKR------RGLVK 1634
Cdd:PRK04863 441 EDWLEEFQAKEQEATEEllsLEQKLSVAQAAHSQFEQAYQLVrkiagevsRSEAWDVARELLRRLREQRhlaeqlQQLRM 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1635 ALRDLEAELDEER----------KQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKD 1694
Cdd:PRK04863 521 RLSELEQRLRQQQraerllaefcKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
836-1344 |
4.60e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 836 RGFLARRNYQKRLQQ--LNAIRIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELRQIRDKLENLSKNS 913
Cdd:TIGR00618 423 QGQLAHAKKQQELQQryAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 914 QEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARL--------------VARKQELEELMQDLESRIEEEEERVNAL 979
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLetseedvyhqltseRKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 980 TSEKKKLQINIQDLeeqleeeeaarqkLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEER--ANDLSQTLAEEE 1057
Cdd:TIGR00618 583 KEDIPNLQNITVRL-------------QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQqcSQELALKLTALH 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1058 EKAKHLAKLKVKHES-TIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLV- 1135
Cdd:TIGR00618 650 ALQLTLTQERVREHAlSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSs 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1136 RIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELldsldttAAQQELRSKREQEVA 1215
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI-------QFFNRLREEDTHLLK 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1216 TLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLE----------KSKQQLEAENADLATELRNVNQSR 1285
Cdd:TIGR00618 803 TLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIThqllkyeecsKQLAQLTQEQAKIIQLSDKLNGIN 882
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1286 QENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAA 1344
Cdd:TIGR00618 883 QIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQGLALLVADAY 941
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1335-1726 |
4.85e-07 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 55.02 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1335 DEAELKASAAIKSagNLESQLTEAQQLLEEETR-QKLALSSKLRQIesekealqeqleedeeaKTNYEKKLAELnftiqE 1413
Cdd:NF033838 53 NESQKEHAKEVES--HLEKILSEIQKSLDKRKHtQNVALNKKLSDI-----------------KTEYLYELNVL-----K 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1414 MKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAandRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDK 1493
Cdd:NF033838 109 EKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATK---KVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1494 VLAEEKAISEQVAQERDaaEREAREKETKVLSLTRELdeafEKIDELETKRKGLQNELDELANT--QGTADKNVHELEKA 1571
Cdd:NF033838 186 KKAELELVKEEAKEPRD--EEKIKQAKAKVESKKAEA----TRLEKIKTDREKAEEEAKRRADAklKEAVEKNVATSEQD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1572 K---RALESQLAEL----KAQNEELEDDLQLTEDA----KLRLEVNMQALRAQFERDIQAKEEQSEEKRRGL-VKALRDL 1639
Cdd:NF033838 260 KpkrRAKRGVLGEPatpdKKENDAKSSDSSVGEETlpspSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYpTNTYKTL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1640 EAELdeerkqraaavaakkkLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERK 1719
Cdd:NF033838 340 ELEI----------------AESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAK 403
|
....*..
gi 158285519 1720 VKTLEAD 1726
Cdd:NF033838 404 RKAAEED 410
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1287-1947 |
5.11e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 55.08 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1287 ENDRRRKQAETQIAELQVKLadvdrvrvelqdKVTKLQQESENITQQLDEAELKASAaIKSAGNLESQLTEAQQLLEEET 1366
Cdd:COG5022 807 GSRKEYRSYLACIIKLQKTI------------KREKKLRETEEVEFSLKAEVLIQKF-GRSLKAKKRFSLLKKETIYLQS 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1367 RQKLALssKLRQIESEKEALQEQLEEdeeAKTNY--EKKLAELNFTIQ-----EMKKRSEEDSDIAKELEESKKKMNKDI 1439
Cdd:COG5022 874 AQRVEL--AERQLQELKIDVKSISSL---KLVNLelESEIIELKKSLSsdlieNLEFKTELIARLKKLLNNIDLEEGPSI 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1440 E-TLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQV------------- 1505
Cdd:COG5022 949 EyVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTkqlkelpvevael 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1506 --AQERDAAEREAREKETKVLSLTRELDEAFEKIdELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELK 1583
Cdd:COG5022 1029 qsASKIISSESTELSILKPLQKLKGLLLLENNQL-QARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRN 1107
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1584 AQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQ--SEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLE 1661
Cdd:COG5022 1108 LVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKlsVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSAL 1187
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1662 GDLKDMEATLEMNNKvKEDALKQAKK------LQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLS 1735
Cdd:COG5022 1188 YDEKSKLSSSEVNDL-KNELIALFSKifsgwpRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLN 1266
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1736 SSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLelmVDRNRKAQLTIEQLTTELATEK 1815
Cdd:COG5022 1267 SIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSE---ELDDWCREFEISDVDEELEELI 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1816 SNSQNNETLKCGLERLnKELKAKLSEQETALRTKLKaataaSEAKNLNLEKQLENETKERLAVQKANRKLekrikELTMN 1895
Cdd:COG5022 1344 QAVKVLQLLKDDLNKL-DELLDACYSLNPAEIQNLK-----SRYDPADKENNLPKEILKKIEALLIKQEL-----QLSLE 1412
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1896 IEDErrhADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECED 1947
Cdd:COG5022 1413 GKDE---TEVHLSEIFSEEKSLISLDRNSIYKEEVLSSLSALLTKEKIALLD 1461
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1043-1340 |
5.98e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1043 EERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETE---------VADLKEQINERR 1113
Cdd:pfam02029 25 EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALerqkefdptIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1114 MQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDlNEELEALKNEl 1193
Cdd:pfam02029 105 ENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTE-NFAKEEVKDE- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1194 ldsldttAAQQELRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKmkgglEKSKQQLEAENAd 1273
Cdd:pfam02029 183 -------KIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE-----EEAEVFLEAEQK- 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 1274 lateLRNVNQSRQENDR--------RRKQAETQIAELQVKLADVDRVRVELQDkvtklQQESENITQQLDEAELK 1340
Cdd:pfam02029 250 ----LEELRRRRQEKESeefeklrqKQQEAELELEELKKKREERRKLLEEEEQ-----RRKQEEAERKLREEEEK 315
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
883-1227 |
7.25e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 883 LEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQEL---- 958
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 959 EELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEED-------------- 1024
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggslls 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1025 ------------VALIEDQNHKLVKEKKLLEERANDLSQTLA----EEEEKAKHLAKLKVKHESTIAELEErLLKDHQQR 1088
Cdd:COG4717 271 liltiagvlflvLGLLALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLE-LLDRIEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1089 QEADRSKRKIETEVadlkeQINERRMQIEE-MQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEA 1167
Cdd:COG4717 350 QELLREAEELEEEL-----QLEELEQEIAAlLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1168 EKLARSKAE-----KQKRDLNEELEALKNEL------LDSLDTTAAQQELRSKREQEVATLKKTLEDESAN 1227
Cdd:COG4717 425 LDEEELEEEleeleEELEELEEELEELREELaeleaeLEQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1324-1686 |
7.35e-07 |
|
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: 54.36 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1324 QQESENITQQLDEAELKASAAIKSagnlesqlTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNyekk 1403
Cdd:pfam17380 280 HQKAVSERQQQEKFEKMEQERLRQ--------EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERE---- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1404 lAELNFTIQEMKKRSEE---DSDIAKELEEskkkmnkdIETLQRQIQELQAANDRldkskkkIQSELEDAtieldtQRTK 1480
Cdd:pfam17380 348 -RELERIRQEERKRELErirQEEIAMEISR--------MRELERLQMERQQKNER-------VRQELEAA------RKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1481 VLELEKKQKnfdkvLAEEKAISEQVAQERDaaerEAREKETKVLSLTRELDeaFEKIDELETKRkglQNELDELANTQGT 1560
Cdd:pfam17380 406 ILEEERQRK-----IQQQKVEMEQIRAEQE----EARQREVRRLEEERARE--MERVRLEEQER---QQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1561 ADKNVHELEKAKRalESQLAElKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFErdiQAKEEQSEEKRRGLVKALRDLE 1640
Cdd:pfam17380 472 RKRKKLELEKEKR--DRKRAE-EQRRKILEKELEERKQAMIEEERKRKLLEKEME---ERQKAIYEEERRREAEEERRKQ 545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 158285519 1641 AELdEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAK 1686
Cdd:pfam17380 546 QEM-EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1431-1698 |
7.63e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 54.26 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1431 SKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKvleleKKQKNFDKvlaeekAISEQVAQERD 1510
Cdd:pfam05667 245 RTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGL-----TKGSRFTH------TEKLQFTNEAP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1511 AAereareketkvlslTRELDEAFEKIDELETKRK----GLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQN 1586
Cdd:pfam05667 314 AA--------------TSSPPTKVETEEELQQQREeeleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1587 EELEDDLQLTEDAKLRL---EVNMQALRAQFE---RDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKL 1660
Cdd:pfam05667 380 EELEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKEL 459
|
250 260 270
....*....|....*....|....*....|....*...
gi 158285519 1661 EGDLKDMEATLemnnKVKEDALKQakkLQAQIKDAIRD 1698
Cdd:pfam05667 460 REKIKEVAEEA----KQKEELYKQ---LVAEYERLPKD 490
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1173-1562 |
7.74e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1173 SKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHESTlmdmrHKHAQEISSINEQLEN 1252
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA-----SDHLNLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1253 LKKMKGGLEKSKQQLEAENADLAtelrNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQEseniTQ 1332
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVE----EADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQA----VQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1333 QLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFtiQ 1412
Cdd:PRK04863 422 ALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVA--R 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1413 EMKKRSEEDSDIAKELEESKKKMNkdieTLQRQIQELQAANDRLDKSKKKI-----------------QSELEDATIELD 1475
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLS----ELEQRLRQQQRAERLLAEFCKRLgknlddedeleqlqeelEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1476 TQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAER----------EAREKETKVLSLTRELDEAFEKIDELETKRK 1545
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefeDSQDVTEYMQQLLERERELTVERDELAARKQ 655
|
410
....*....|....*..
gi 158285519 1546 GLQNELDELANTQGTAD 1562
Cdd:PRK04863 656 ALDEEIERLSQPGGSED 672
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1122-1966 |
7.88e-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: 54.67 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1122 QLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTA 1201
Cdd:TIGR00606 183 RYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1202 AQQELRS------KREQEVATLKKTLEDESAN----HESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAEN 1271
Cdd:TIGR00606 263 KIMKLDNeikalkSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1272 ADLatelrnvnqsrqENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESEN-------ITQQLDEAELKASAA 1344
Cdd:TIGR00606 343 TEL------------LVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSerqiknfHTLVIERQEDEAKTA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1345 IKSAGNLESQLTEAQQLLEEETRQKLALSsklRQIESEKEAlqeqleedeeaktnYEKKLAELNFTIQE-------MKKR 1417
Cdd:TIGR00606 411 AQLCADLQSKERLKQEQADEIRDEKKGLG---RTIELKKEI--------------LEKKQEELKFVIKElqqlegsSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1418 SEEDSDIAKELEE-SKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTqRTKVLELEKKQKNFDKvla 1496
Cdd:TIGR00606 474 LELDQELRKAERElSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT-RTQMEMLTKDKMDKDE--- 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1497 eekaiseqvaQERDAAEREAREketkVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQgtadKNVHELEKAKRALE 1576
Cdd:TIGR00606 550 ----------QIRKIKSRHSDE----LTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN----KELASLEQNKNHIN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1577 SQLAELKAQNEELEDDLqltedaklrlevnmqalraqferdIQAKEEQSEEKRrglvkaLRDLEAELDEERKQRAAAVAA 1656
Cdd:TIGR00606 612 NELESKEEQLSSYEDKL------------------------FDVCGSQDEESD------LERLKEEIEKSSKQRAMLAGA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1657 KKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDairdaEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSS 1736
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD-----LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1737 SERARRAaegerDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLtieQLTTELATEKS 1816
Cdd:TIGR00606 737 SIIDLKE-----KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERF---QMELKDVERKI 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1817 NSQNNETLKCGLERLNKELKAKLSEQETALRTklkaatAASEAKNLNLEKQLENETKERLAVQKANRKLEKrikeltMNI 1896
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDT------VVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK------LQI 876
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1897 EDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSR----EVNALKSKL 1966
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKkaqdKVNDIKEKV 950
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1079-1363 |
7.92e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 53.00 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1079 ERLLKDHQQRQEADRSKRK--IETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAkaaaqktQRELES 1156
Cdd:pfam00038 31 ETKISELRQKKGAEPSRLYslYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNL-------RTSAEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1157 QLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNElldsldttaaqqelrskREQEVATLKKTLEDESANHEstlMDMR 1236
Cdd:pfam00038 104 DLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVE---MDAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1237 HKH--AQEISSINEQLENLkkmkggLEKSKQQLEAEnadLATELRNVNQSRQENDRRRKQAETQIAELQVKladVDRVRV 1314
Cdd:pfam00038 164 RKLdlTSALAEIRAQYEEI------AAKNREEAEEW---YQSKLEELQQAAARNGDALRSAKEEITELRRT---IQSLEI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 158285519 1315 ELQDkvtkLQQESENITQQLDEAELKASAAIKSA----GNLESQLTEAQQLLE 1363
Cdd:pfam00038 232 ELQS----LKKQKASLERQLAETEERYELQLADYqeliSELEAELQETRQEMA 280
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1039-1907 |
8.14e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1039 KKLLEERANDLSQTLAEEEEKAKHLAKLKVKHEStiaeleerlLKDHQQR-QEADRSKRKIETEVADLKE---QINERRM 1114
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQA---------ASDHLNLvQTALRQQEKIERYQADLEEleeRLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1115 QIEEMQQQLVKREEELAQTlvrideesaakaaaQKTQRELESQLAEIQEDLEAEklarskaekQKRDL--NEELEALK-- 1190
Cdd:PRK04863 370 VVEEADEQQEENEARAEAA--------------EEEVDELKSQLADYQQALDVQ---------QTRAIqyQQAVQALEra 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1191 NELLDSLDTTAA-----QQELRSKrEQEVatlkktleDESANHESTLMDMrhkhAQEISSINEQ-LENLKKMKGGLEKSk 1264
Cdd:PRK04863 427 KQLCGLPDLTADnaedwLEEFQAK-EQEA--------TEELLSLEQKLSV----AQAAHSQFEQaYQLVRKIAGEVSRS- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1265 qqlEAENADLATELRNVNQsrqendrrRKQAEtQIAELQVKLADVDRvRVELQDKVTKLQQESE--NITQQLDEAELKAs 1342
Cdd:PRK04863 493 ---EAWDVARELLRRLREQ--------RHLAE-QLQQLRMRLSELEQ-RLRQQQRAERLLAEFCkrLGKNLDDEDELEQ- 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1343 aaiksagnLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELnftiQEMKKRSEEDS 1422
Cdd:PRK04863 559 --------LQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARL----REQSGEEFEDS 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1423 DIAKELeeskkkmnkdIETLQRQIQELQAANDRLDKSKKKIQSELEdatiELDTQRTKVLE-LEKKQKNFDKVLAEEkaI 1501
Cdd:PRK04863 627 QDVTEY----------MQQLLERERELTVERDELAARKQALDEEIE----RLSQPGGSEDPrLNALAERFGGVLLSE--I 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1502 SEQVAQErDAAEREAREKETKVLSLTRELDEAFEKIDELEtkrkglqNELDELANTQGTADK------NVHELEKA---- 1571
Cdd:PRK04863 691 YDDVSLE-DAPYFSALYGPARHAIVVPDLSDAAEQLAGLE-------DCPEDLYLIEGDPDSfddsvfSVEELEKAvvvk 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1572 ------------------KRALESQLAELKAQNEELEddlqlTEDAKLRLEVN-MQALRAQFERDIQ-----AKEEQSEE 1627
Cdd:PRK04863 763 iadrqwrysrfpevplfgRAAREKRIEQLRAEREELA-----ERYATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEA 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1628 KRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDAL-KQAKKLQAQIKDA------IRDAE 1700
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLaDRVEEIREQLDEAeeakrfVQQHG 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1701 EAKAAKEELAAISKESERKVKTLEADLMQLTEDLS---------SSERARRAAEGERD--ELLEEINSNSSK--GSLMID 1767
Cdd:PRK04863 918 NALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRdakqqafalTEVVQRRAHFSYEDaaEMLAKNSDLNEKlrQRLEQA 997
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1768 EKRRLEARIAAleeeleeeqsnlelmvdRNRKAQLTieQLTTELATEKSNSQN-NETLKCGLERLNK---ELKAKLSEQE 1843
Cdd:PRK04863 998 EQERTRAREQL-----------------RQAQAQLA--QYNQVLASLKSSYDAkRQMLQELKQELQDlgvPADSGAEERA 1058
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1844 TALRTKLKAATAASEAKNLNLEKQLENETKERlavqkanRKLEKRIKELTMNIEDERRHADQYK 1907
Cdd:PRK04863 1059 RARRDELHARLSANRSRRNQLEKQLTFCEAEM-------DNLTKKLRKLERDYHEMREQVVNAK 1115
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1186-1649 |
1.19e-06 |
|
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: 53.59 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1186 LEALKNELldsldttaAQQELRSKREQ-----EVATLKKTLEDESANHESTLMDMRHKHAQEissiNEQLENLKKMKGGL 1260
Cdd:pfam05557 11 LSQLQNEK--------KQMELEHKRARielekKASALKRQLDRESDRNQELQKRIRLLEKRE----AEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1261 EKSKQQLEAenadlatelrnVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELK 1340
Cdd:pfam05557 79 RLKKKYLEA-----------LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1341 ASAAIKSAGNLESQlteaQQLLEEETRQKLALSSKLRQIESEKEalqeqleedeeaktnyekklaELNFTIQEMKKRSEE 1420
Cdd:pfam05557 148 ASEAEQLRQNLEKQ----QSSLAEAEQRIKELEFEIQSQEQDSE---------------------IVKNSKSELARIPEL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1421 DSDIAKELEESKK--KMNKDIETLQRQIQELQAANDRLDKSKKKIqseledATIELDTQR--TKVLELEKKQKNFDKVLA 1496
Cdd:pfam05557 203 EKELERLREHNKHlnENIENKLLLKEEVEDLKRKLEREEKYREEA------ATLELEKEKleQELQSWVKLAQDTGLNLR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1497 EEKAISEQVAQ----------ERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDEL------------ 1554
Cdd:pfam05557 277 SPEDLSRRIEQlqqreivlkeENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvllltkerd 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1555 ---------------ANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFErdiQ 1619
Cdd:pfam05557 357 gyrailesydkeltmSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQES---L 433
|
490 500 510
....*....|....*....|....*....|
gi 158285519 1620 AKEEQSEEKRRGLVKALRDLEAELDEERKQ 1649
Cdd:pfam05557 434 ADPSYSKEEVDSLRRKLETLELERQRLREQ 463
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1235-1649 |
1.48e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.30 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1235 MRHKHAQEISSineqlenlkkmkggLEKSKQQLeaENADLATELRNVN------QSRQENDRRRKQAETQIAelqVKLAD 1308
Cdd:PRK04778 23 LRKRNYKRIDE--------------LEERKQEL--ENLPVNDELEKVKklnltgQSEEKFEEWRQKWDEIVT---NSLPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1309 VDRVRVELQD-----KVTKLQQESENITQQLDEAElkasaaiksaGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEK 1383
Cdd:PRK04778 84 IEEQLFEAEElndkfRFRKAKHEINEIESLLDLIE----------EDIEQILEELQELLESEEKNREEVEQLKDLYRELR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1384 EALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSE-----EDSDIAKELEESKKKMNKDIE-----------TLQRQIQ 1447
Cdd:PRK04778 154 KSLLANRFSFGPALDELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEeipellkelqtELPDQLQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1448 ELQAANDRLDKSK-----KKIQSELEDATIELDTQRTKVLELEkkqknFDKVLAEEKAISEQVAQERDAAERE--AR--- 1517
Cdd:PRK04778 234 ELKAGYRELVEEGyhldhLDIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEIQERIDQLYDILEREvkARkyv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1518 EKETKVLSltreldeafEKIDELETKRKGLQNELDELANTQGTADknvHELEKAkRALESQLAELKAQneeLEDDLQLTE 1597
Cdd:PRK04778 309 EKNSDTLP---------DFLEHAKEQNKELKEEIDRVKQSYTLNE---SELESV-RQLEKQLESLEKQ---YDEITERIA 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 1598 DAKLR---LEVNMQALRAQFErDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQ 1649
Cdd:PRK04778 373 EQEIAyseLQEELEEILKQLE-EIEKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
807-1509 |
1.49e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 807 FFRAGVLahleEERD--YKITDLIVNFQAFCRgflARRNYQKRLQQLNAIRIIQRNCAAYLKLRN-----------WQWW 873
Cdd:COG4913 212 FVREYML----EEPDtfEAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 874 RLYTKVKpLL--EVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAmeeKTHLAEQLQAEIElcaEAEEGRARL 951
Cdd:COG4913 285 FAQRRLE-LLeaELEELRAELARLEAELERLEARLDALREELDELEAQIRGN---GGDRLEQLEREIE---RLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 952 VARKQELEELMQDLESRIEEEEERVNALtseKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQ 1031
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1032 N----HKLVKEKKLLEERAN----------DLSQTLAEEE------EKA------------KHLAK-------LKVKHES 1072
Cdd:COG4913 435 KsnipARLLALRDALAEALGldeaelpfvgELIEVRPEEErwrgaiERVlggfaltllvppEHYAAalrwvnrLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1073 TIAELEERLLKDHQQRQEADRSKRKIETEVAD----LKEQINERRMQIeemqqqLVKREEELAQT--------LVRIDEE 1140
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSLAGKLDFKPHPfrawLEAELGRRFDYV------CVDSPEELRRHpraitragQVKGNGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1141 SAAKAAAQKTQREL------ESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEAlknelLDSLDTTAAQQELRSKREQEV 1214
Cdd:COG4913 589 RHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDA-----LQERREALQRLAEYSWDEIDV 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1215 ATLkktledesanhestlmdmrhkhAQEISSINEQLENLKKMKGGLEKSKQQLEAenadlatelrnVNQSRQENDRRRKQ 1294
Cdd:COG4913 664 ASA----------------------EREIAELEAELERLDASSDDLAALEEQLEE-----------LEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1295 AETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKL-ALS 1373
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEeELE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1374 SKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELnftiqemkkrseEDSDIAK---ELEESKKK-MNKDIETLQRQI-QE 1448
Cdd:COG4913 791 RAMRAFNREWPAETADLDADLESLPEYLALLDRL------------EEDGLPEyeeRFKELLNEnSIEFVADLLSKLrRA 858
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1449 LQAANDRLDkskkKIQSEL------EDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQER 1509
Cdd:COG4913 859 IREIKERID----PLNDSLkripfgPGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEAR 921
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1030-1226 |
1.76e-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: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1030 DQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQI 1109
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1110 NERRmqiEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEAL 1189
Cdd:COG4942 100 EAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 158285519 1190 KNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESA 1226
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
884-1139 |
1.86e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKLENLSKnsQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQ 963
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 964 DLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLE 1043
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1044 ERANDLSQTLAEEEEKAKHLAKLKvKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQL 1123
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
250
....*....|....*.
gi 158285519 1124 VKREEELAQTLVRIDE 1139
Cdd:TIGR02169 996 AKLEEERKAILERIEE 1011
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1435-1633 |
2.23e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1435 MNKDIETLqRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAE-EKAISEQVAQERDAAE 1513
Cdd:COG1579 2 MPEDLRAL-LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRlELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1514 REAREKETKVL-SLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKnvhELEKAKRALESQLAELKAQNEELEDD 1592
Cdd:COG1579 81 QLGNVRNNKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEA---ELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 158285519 1593 LQltedaklRLEVNMQALRAQFERDIQAKEEQSEEKRRGLV 1633
Cdd:COG1579 158 LE-------ELEAEREELAAKIPPELLALYERIRKRKNGLA 191
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
884-1313 |
3.12e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELcaeaeegrarLVARKQELEELMQ 963
Cdd:PRK01156 350 DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA----------IKKELNEINVKLQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 964 DLESRIEEEEERVNALTSEKKKLQINIQdleeqleeEEAARQKLQLEKVQLDAklkkmEEDVALIEDQNHKLVKekklLE 1043
Cdd:PRK01156 420 DISSKVSSLNQRIRALRENLDELSRNME--------MLNGQSVCPVCGTTLGE-----EKSNHIINHYNEKKSR----LE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1044 ERANDLSQTLAEEEEKAKHLAKLK---VKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINE--RRMQIEE 1118
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKeylESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNryKSLKLED 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1119 MQQQLVKREEELAQ-TLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKlarSKAEKQKRDLNEELEALKNELLDSL 1197
Cdd:PRK01156 563 LDSKRTSWLNALAViSLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEIQ 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1198 DTTAAQQELRSKreqeVATLKKtledesanhESTLMDMRHKHAQEISS-INEQLENLKKMKGGLEKSKQQLEAENADLAT 1276
Cdd:PRK01156 640 ENKILIEKLRGK----IDNYKK---------QIAEIDSIIPDLKEITSrINDIEDNLKKSRKALDDAKANRARLESTIEI 706
|
410 420 430
....*....|....*....|....*....|....*..
gi 158285519 1277 ELRNVNQSRQENDRRRKQAEtQIAELQVKLADVDRVR 1313
Cdd:PRK01156 707 LRTRINELSDRINDINETLE-SMKKIKKAIGDLKRLR 742
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1411-1593 |
4.27e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1411 IQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELeKKQKN 1490
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1491 FDKVLAEEkaiseqvaqerDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANtqgtadknvhELEK 1570
Cdd:COG1579 91 YEALQKEI-----------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA----------ELDE 149
|
170 180
....*....|....*....|...
gi 158285519 1571 AKRALESQLAELKAQNEELEDDL 1593
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKI 172
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1104-1640 |
4.76e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1104 DLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLE-AEKLARSKAEKQKRDL 1182
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDmKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1183 NEELEALKNELLDSLDTTAAQQELRSKREQ--EVATLKKTLED-----ESANHESTLMDMRHKHAQEISSINEQLENLKK 1255
Cdd:PRK01156 267 MELEKNNYYKELEERHMKIINDPVYKNRNYinDYFKYKNDIENkkqilSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1256 MKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKL-----------ADVDRVRVELQD---KVT 1321
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILkiqeidpdaikKELNEINVKLQDissKVS 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1322 KLQQESENITQQLDeaELKASAAIKSAGNL----ESQLTE--AQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEE 1395
Cdd:PRK01156 427 SLNQRIRALRENLD--ELSRNMEMLNGQSVcpvcGTTLGEekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1396 AKTNYEKKlaELNFTIQEMKKRSEEDSDIAK------ELEESKKKMNKDIETLQR-QIQELQAANDRLDKSKKKIQSele 1468
Cdd:PRK01156 505 RKEYLESE--EINKSINEYNKIESARADLEDikikinELKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISL--- 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1469 datIELDTQRTKVLELEKKQKNFDKVLAEekaISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQ 1548
Cdd:PRK01156 580 ---IDIETNRSRSNEIKKQLNDLESRLQE---IEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1549 NELDELAntqgtadkNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSE-- 1626
Cdd:PRK01156 654 NYKKQIA--------EIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINEtl 725
|
570
....*....|....
gi 158285519 1627 EKRRGLVKALRDLE 1640
Cdd:PRK01156 726 ESMKKIKKAIGDLK 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1209-1942 |
5.55e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1209 KREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINE-QLENLK---KMKGGLEKSKQQLEAENADlatelRNVNQS 1284
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIKENNAT-----RHLCNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1285 RQENDRRRKQaetQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAgnlESQLTEAQQLLEE 1364
Cdd:pfam05483 160 LKETCARSAE---KTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKED---HEKIQHLEEEYKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1365 ETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAE-LNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQ 1443
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEkTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1444 RQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEkaiseqvaqerdaaEREAREKETKV 1523
Cdd:pfam05483 314 ALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTE--------------QQRLEKNEDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1524 LSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHElekaKRALESQLAELKAQNEELEDDLQLTEDAKLRL 1603
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1604 EVNMQALRAQFERDIQAKEEQSEEKRRGLVKALrDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALK 1683
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNI-ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1684 QAKKLQaQIKDAIRDAEEAKAAKEELAaiSKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGS 1763
Cdd:pfam05483 535 QIENLE-EKEMNLRDELESVREEFIQK--GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1764 LMIDEKRRLEARIAALEEELEEEqsnlelmvdrnrkaQLTIEQLTTELATEKSNSQNNetlkcgLERLNKELKAKLSEQE 1843
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAY--------------EIKVNKLELELASAKQKFEEI------IDNYQKEIEDKKISEE 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1844 TALRTKLKAATAASEAKNLN--LEKQLENETKERLAVQKANRK-----LEKRIKELTM--NIEDERRHADQYKE-QIEKA 1913
Cdd:pfam05483 672 KLLEEVEKAKAIADEAVKLQkeIDKRCQHKIAEMVALMEKHKHqydkiIEERDSELGLykNKEQEQSSAKAALEiELSNI 751
|
730 740
....*....|....*....|....*....
gi 158285519 1914 NNRMKTLKRNLDEAEEEIQKektLKRKAQ 1942
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEK---LKMEAK 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1325-1698 |
5.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1325 QESENITQQLDEAELKAS---AAIKSAGNLESQLTEAQQLLEE--ETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTN 1399
Cdd:COG4717 71 KELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1400 YEKKLAELNFTIQEMKKRSEEDSDIAKELEEskkKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRT 1479
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1480 KVLELEKKQKNFD--KVLAEEK-------AISEQVAQERDAAEREAREKETKVLSL-------------TRELDEAFEKI 1537
Cdd:COG4717 228 ELEQLENELEAAAleERLKEARlllliaaALLALLGLGGSLLSLILTIAGVLFLVLgllallflllareKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1538 DELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLtEDAKLRLEVNMQALRAQFERD 1617
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-EELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1618 IQAKEEQSEEKRRgLVKALRDLEAELDEERK--QRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDA 1695
Cdd:COG4717 387 LRAALEQAEEYQE-LKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
...
gi 158285519 1696 IRD 1698
Cdd:COG4717 466 EED 468
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
885-1486 |
6.38e-06 |
|
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: 51.29 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 885 VTKQEEKLVQKEDELRQIRDKLENLSKNS-QEYEKKYQQAMEekthLAEQLQAEIELCAEAEEGRARLVARkqelEELMQ 963
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLRETSlQQKMRLEAQAME----LDALAVAEKAGQAEAEGLRAALAGA----EMVRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 964 DLESRIEEEEERVNALTSEkkklQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQnhklvKEKKLLE 1043
Cdd:pfam07111 133 NLEEGSQRELEEIQRLHQE----QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----KEAELLR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1044 eraNDLSQTLAEEEEKAKHLAKL-KVKHESTIAELEERLLKdhQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQ 1122
Cdd:pfam07111 204 ---KQLSKTQEELEAQVTLVESLrKYVGEQVPPEVHSQTWE--LERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1123 LVKREEELAQTLVRIDE-ESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELealknelldsldtta 1201
Cdd:pfam07111 279 LALQEEELTRKIQPSDSlEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL--------------- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1202 aqQELRSKREQEVATLKKTLEDESANHESTLM-------------DMRHKHAQEISSINEQLE-----------NLKKMK 1257
Cdd:pfam07111 344 --QEQVTSQSQEQAILQRALQDKAAEVEVERMsakglqmelsraqEARRRQQQQTASAEEQLKfvvnamsstqiWLETTM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1258 GGLEKSKQQLEAENADLATELRNVN-------------QSRQENDRRRKQAETQIAELQVKLADV----DRVRVELQDKV 1320
Cdd:pfam07111 422 TRVEQAVARIPSLSNRLSYAVRKVHtikglmarkvalaQLRQESCPPPPPAPPVDADLSLELEQLreerNRLDAELQLSA 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1321 TKLQQESENITQQlDEAElkasaaiksagnlESQLTE-AQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTN 1399
Cdd:pfam07111 502 HLIQQEVGRAREQ-GEAE-------------RQQLSEvAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQE 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1400 YEKKLAELNFTIQEM-----KKRSEEDSDIAKELEESKKKMNKDIETLqRQIQELQAANDRLDKSKKKIQSELEDATIEL 1474
Cdd:pfam07111 568 LTQQQEIYGQALQEKvaeveTRLREQLSDTKRRLNEARREQAKAVVSL-RQIQHRATQEKERNQELRRLQDEARKEEGQR 646
|
650
....*....|..
gi 158285519 1475 DTQRTKVLELEK 1486
Cdd:pfam07111 647 LARRVQELERDK 658
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1117-1370 |
6.93e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1117 EEMQQQLvkreEELAQTLVRIDEESAAKAAAQKTQRELEsQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDS 1196
Cdd:PRK11281 39 ADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLD-KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1197 LDTTAAQQELR------SKREQEVATLKKTLEDesANHESTLMDMRHKHAQ-EISS-------INEQLENLKKMKGGLEK 1262
Cdd:PRK11281 114 TRETLSTLSLRqlesrlAQTLDQLQNAQNDLAE--YNSQLVSLQTQPERAQaALYAnsqrlqqIRNLLKGGKVGGKALRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1263 S-KQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKV-TKLQQESENITQQLDEAELK 1340
Cdd:PRK11281 192 SqRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAInSKRLTLSEKTVQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*...
gi 158285519 1341 ASA------AIKSAGNLE-SQ-LTEAQQLLEEETRQKL 1370
Cdd:PRK11281 272 ARIqanplvAQELEINLQlSQrLLKATEKLNTLTQQNL 309
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
874-1198 |
6.95e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 874 RLYTKVKPLLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVA 953
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 954 RKQELEELMQDLESRiEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDvaliedqnH 1033
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDE-KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED--------K 1743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1034 KLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKvkhESTIAELEERllKDHQQRQEADRSKRKIETEVADLKEQINERR 1113
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIEEELDE--EDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1114 MQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKlarskaEKQKRDLNEELEALKNEL 1193
Cdd:PTZ00121 1819 LVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK------DLKEDDEEEIEEADEIEK 1892
|
....*
gi 158285519 1194 LDSLD 1198
Cdd:PTZ00121 1893 IDKDD 1897
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1054-1623 |
8.14e-06 |
|
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: 50.98 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1054 AEEEEKAKHLAKLKvkheSTIAELEERLLKDHQQRQEADRSKRKI-------------ETEVADLKEQINERRMQIEEMQ 1120
Cdd:pfam10174 123 SEHERQAKELFLLR----KTLEEMELRIETQKQTLGARDESIKKLlemlqskglpkksGEEDWERTRRIAEAEMQLGHLE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1121 QQLVKREEELAQTLVRIDEESAAKAAAQKTQrelesqlaEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLdsLDTT 1200
Cdd:pfam10174 199 VLLDQKEKENIHLREELHRRNQLQPDPAKTK--------ALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGL--LHTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1201 AAQQELR-----------------------SKREQEVATLKKTLE------DESANH-----ES-TLMDMRHKHAQ-EIS 1244
Cdd:pfam10174 269 DREEEIKqmevykshskfmknkidqlkqelSKKESELLALQTKLEtltnqnSDCKQHievlkESlTAKEQRAAILQtEVD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1245 SINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQ 1324
Cdd:pfam10174 349 ALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQ 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1325 QESENITQQLdeaelkasaaiksaGNLESQLTEAQQLLEEETRQKlalssklrqiESEKEALQEQLEEDEEAKTNYEKKL 1404
Cdd:pfam10174 429 TDSSNTDTAL--------------TTLEEALSEKERIIERLKEQR----------EREDRERLEELESLKKENKDLKEKV 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1405 AELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELD-TQRTKVLE 1483
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEiNDRIRLLE 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1484 LE---------KKQKNFDKVLaeekAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELET--KRKGLQNELD 1552
Cdd:pfam10174 565 QEvarykeesgKAQAEVERLL----GILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQemKKKGAQLLEE 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1553 ELANTQGTADKNVH--------ELEKAKRALESQLAELKAQNEEL-EDDLQLTedaKLRLEvnmqaLRAQFERDIQAKEE 1623
Cdd:pfam10174 641 ARRREDNLADNSQQlqleelmgALEKTRQELDATKARLSSTQQSLaEKDGHLT---NLRAE-----RRKQLEEILEMKQE 712
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1155-1385 |
8.51e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1155 ESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESAnhestLMD 1234
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE-----ELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1235 MRHKHAQEISSINEQLENLkkmkgglekskqqLEAEN-ADLATELRNVNQ-SRQEND------RRRKQAETQIAELQVKL 1306
Cdd:COG3883 90 ERARALYRSGGSVSYLDVL-------------LGSESfSDFLDRLSALSKiADADADlleelkADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1307 ADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEA 1385
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
883-1336 |
1.08e-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: 50.49 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 883 LEVTKQEEKLVQKEDELRQIRDKLEN----LSKNSQEYEKKYQQaMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQEL 958
Cdd:pfam05483 349 FVVTEFEATTCSLEELLRTEQQRLEKnedqLKIITMELQKKSSE-LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 959 EELMQDLESRIEEEEERVNalTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEedvalIEDQNHKLVKE 1038
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQ--AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLE 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1039 KKLLEERANDLSQTLAEEEEKAKHLAKLkvkhestiaelEERLLKDHQQRQEADRSKR-KIETEVADLKEQINERRMQIE 1117
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQ-----------EERMLKQIENLEEKEMNLRdELESVREEFIQKGDEVKCKLD 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1118 EMQQQLVKREEELaqtLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEeLEALKNELLDSL 1197
Cdd:pfam05483 570 KSEENARSIEYEV---LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNA-YEIKVNKLELEL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1198 DTTaaqqelRSKREQEVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLE-------NLKKMKGGLEKSKQQLEAE 1270
Cdd:pfam05483 646 ASA------KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEidkrcqhKIAEMVALMEKHKHQYDKI 719
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1271 NADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDE 1336
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1523-1764 |
1.25e-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: 49.76 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1523 VLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLR 1602
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1603 LEVNMQALRAQFERDIQAKEEQSeekRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEgDLKDMEATLEMNNKVKEDAL 1682
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE-QAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1683 KQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTED---LSSSERARRAAEGERDELLEEINSNS 1759
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEaeeLEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 158285519 1760 SKGSL 1764
Cdd:COG4942 251 LKGKL 255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1398-1967 |
1.32e-05 |
|
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: 50.43 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1398 TNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETL-QRQIQElqAANDRLDKSKKKIQSELEDATIELDT 1476
Cdd:TIGR00606 182 TRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQItSKEAQL--ESSREIVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1477 QRTKVLELEKKQKNFDKVLAEEKAISEQVAQERD----AAEREARE----KETKVLSLTRELDEAFEKIDELETKRKGLQ 1548
Cdd:TIGR00606 260 NLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEkvfqGTDEQLNDlyhnHQRTVREKERELVDCQRELEKLNKERRLLN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1549 NELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEEleDDLQLTEDAKLrlevnmqalraQFERDIQAKEEQSEEK 1628
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL--DGFERGPFSER-----------QIKNFHTLVIERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1629 RRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEE 1708
Cdd:TIGR00606 407 AKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1709 LAAISKESerKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEK------RRLEARIAALEEE 1782
Cdd:TIGR00606 487 LSKAEKNS--LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMdkdeqiRKIKSRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1783 LEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKcglERLNKELKaKLSEQETALRTKL--KAATAASEAK 1860
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNK---NHINNELE-SKEEQLSSYEDKLfdVCGSQDEESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1861 NLNLEKQLENETKERLAVQKANR------------------------KLEKRIKELTMNIEDERRHADQYKEQIEKannR 1916
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAvysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTES---E 717
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1917 MKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKLS 1967
Cdd:TIGR00606 718 LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
884-1061 |
1.32e-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: 49.76 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKL----ENLSKNSQEYEKKYQQAMEEKTHLAEQLQA--------EIELCAEAEEGrARL 951
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELaaleAELAELEKEIAELRAELEAQKEELAELLRAlyrlgrqpPLALLLSPEDF-LDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 952 VARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQ 1031
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
170 180 190
....*....|....*....|....*....|
gi 158285519 1032 NHKLVKEKKLLEERANDLSQTLAEEEEKAK 1061
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
886-1582 |
1.38e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.44 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 886 TKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAME----EKTHLAEQLQAEI----------ELCAEAEEGRARL 951
Cdd:TIGR01612 930 KESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDntliDKINELDKAFKDAslndyeaknnELIKYFNDLKANL 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 952 VARKQ--------ELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLE-EEEAARQKLQLEKVQLD-AKLKKM 1021
Cdd:TIGR01612 1010 GKNKEnmlyhqfdEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIgKNIELLNKEILEEAEINiTNFNEI 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1022 EEDVAL------IEDQNHKLVKEKKLLEERANDLSQTLaeeEEKAKHLAKLKVKHESTIAELEERL--LKDHQQRQEADR 1093
Cdd:TIGR01612 1090 KEKLKHynfddfGKEENIKYADEINKIKDDIKNLDQKI---DHHIKALEEIKKKSENYIDEIKAQIndLEDVADKAISND 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1094 SKRKIETEVADLKEQINERRMQIEEMQQQLVKREE-ELAQT--------------------LVRIDEESAAKAAAQKTQR 1152
Cdd:TIGR01612 1167 DPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEiEKDKTsleevkginlsygknlgklfLEKIDEEKKKSEHMIKAME 1246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1153 ELESQLAEIQE---DLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSK---------REQEVATLKKT 1220
Cdd:TIGR01612 1247 AYIEDLDEIKEkspEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKslkiiedfsEESDINDIKKE 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1221 LED---ESANHESTLmdmrHKHAQEISSINE--QLENLKKMKGGLEKSKQQLEAENADLATELRNVNQ--SRQENDRRRK 1293
Cdd:TIGR01612 1327 LQKnllDAQKHNSDI----NLYLNEIANIYNilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKliKKIKDDINLE 1402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1294 QAETQIaELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLE---------- 1363
Cdd:TIGR01612 1403 ECKSKI-ESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKikkdnatndh 1481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1364 ----EETRQKLALSSKL--------RQIESEKEALQEQLEE---------DEEAKTNYEKKLAELNFTIQEMKkrsEEDS 1422
Cdd:TIGR01612 1482 dfniNELKEHIDKSKGCkdeadknaKAIEKNKELFEQYKKDvtellnkysALAIKNKFAKTKKDSEIIIKEIK---DAHK 1558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1423 DIAKELEESKKKMNKdIETLQRQIQELQAANDRLDKSKKKIQSELEDAtieldtqRTKVLELEKKQKNFDKVLAEEKAIS 1502
Cdd:TIGR01612 1559 KFILEAEKSEQKIKE-IKKEKFRIEDDAAKNDKSNKAAIDIQLSLENF-------ENKFLKISDIKKKINDCLKETESIE 1630
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1503 EQVAQ-ERDAAEREAREKETKVLSL----------TRELDEAFEKIDELETKRKGLQNELDE---------LANTQGTAD 1562
Cdd:TIGR01612 1631 KKISSfSIDSQDTELKENGDNLNSLqefleslkdqKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigiIEKIKEIAI 1710
|
810 820
....*....|....*....|
gi 158285519 1563 KNVHELEKAKRALESQLAEL 1582
Cdd:TIGR01612 1711 ANKEEIESIKELIEPTIENL 1730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1536-1970 |
1.66e-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: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1536 KIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFE 1615
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1616 RDIQAKEEQSEEkrrglvkaLRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVK---EDALKQAKKLQAQI 1692
Cdd:TIGR04523 114 NDKEQKNKLEVE--------LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKeelENELNLLEKEKLNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1693 KDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRL 1772
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1773 EARIAALEEELEEEQSNLELMVDRnrkaqltIEQLTTELATEKSNSQNNetlkcglerLNKELKAKLSEQETALR----- 1847
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQ-------LNQLKSEISDLNNQKEQD---------WNKELKSELKNQEKKLEeiqnq 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1848 ---------------TKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEK 1912
Cdd:TIGR04523 330 isqnnkiisqlneqiSQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 1913 ANNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKLSIHK 1970
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1048-1363 |
1.73e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1048 DLSQTLAEEEEKAKHLAKlkvkhESTIAELEERLL--------KDHQQRQEADRSkRKIETEVADLKEQINERRMQIEEM 1119
Cdd:PRK10929 83 ELRQQLNNERDEPRSVPP-----NMSTDALEQEILqvssqlleKSRQAQQEQDRA-REISDSLSQLPQQQTEARRQLNEI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1120 QQQLvkreeelaQTLvriDEESAAKAAAQKTQRELESQLAEIQ-EDLEAEKL--------ARSKAE---KQKRDLNEELE 1187
Cdd:PRK10929 157 ERRL--------QTL---GTPNTPLAQAQLTALQAESAALKALvDELELAQLsannrqelARLRSElakKRSQQLDAYLQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1188 ALKNElLDSLDTTAAQQELRSKR--EQEVATLKKTLEDE-SANHEstLMDMRHKHAQEISSI-------NEQLENLKKMK 1257
Cdd:PRK10929 226 ALRNQ-LNSQRQREAERALESTEllAEQSGDLPKSIVAQfKINRE--LSQALNQQAQRMDLIasqqrqaASQTLQVRQAL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1258 GGLEKSKQQLEAENAdLATELRnVNQSRQENDRRRKQAETQIAELQVKladvdRVRVE-LQDKVTKLQQESENITQQLDE 1336
Cdd:PRK10929 303 NTLREQSQWLGVSNA-LGEALR-AQVARLPEMPKPQQLDTEMAQLRVQ-----RLRYEdLLNKQPQLRQIRQADGQPLTA 375
|
330 340
....*....|....*....|....*..
gi 158285519 1337 AELKAsaaiksagnLESQLTEAQQLLE 1363
Cdd:PRK10929 376 EQNRI---------LDAQLRTQRELLN 393
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1086-1293 |
1.75e-05 |
|
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: 48.99 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1086 QQRQEADRSKrkieTEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDE-ESAAKAAAQKTQRELESQLAEIQED 1164
Cdd:pfam09787 51 ELRQERDLLR----EEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEqLATERSARREAEAELERLQEELRYL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1165 LEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELrskrEQEVATLKKTLEDESANHESTlmdmrhkhAQEIS 1244
Cdd:pfam09787 127 EEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSEL----ENRLHQLTETLIQKQTMLEAL--------STEKN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 158285519 1245 SINEQLENLKKmkgglEKSKQQLEAENadlATELRNVNQSRQENDRRRK 1293
Cdd:pfam09787 195 SLVLQLERMEQ-----QIKELQGEGSN---GTSINMEGISDGEGTRLRN 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1768-1967 |
1.88e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1768 EKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTELATEKSNSQNN-----ETLKCGLERLNKELKAKLSEQ 1842
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekiGELEAEIASLERSIAEKEREL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1843 ETALRT--KLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDE-------RRHADQYKEQIEKA 1913
Cdd:TIGR02169 318 EDAEERlaKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLEKL 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1914 NNRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKLS 1967
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1712-1966 |
2.00e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1712 ISKESERKVKTLEA-------------------------DLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMI 1766
Cdd:TIGR02168 194 ILNELERQLKSLERqaekaerykelkaelrelelallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1767 DEKRRLEARIAALEEELEEEQSNLELM-------VDRNRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKL 1839
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1840 SEQETALrTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIED-----ERRHADQYKEQIEKAN 1914
Cdd:TIGR02168 354 ESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledrrERLQQEIEELLKKLEE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1915 NRMKTLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKL 1966
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
692-719 |
2.08e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 46.95 E-value: 2.08e-05
10 20
....*....|....*....|....*...
gi 158285519 692 SHLYKEQLAKLMDTLRNTNPNFVRCIIP 719
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1483-1643 |
2.31e-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: 49.12 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1483 ELEKKQKNFDKVLAEEKaisEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELAntqgtad 1562
Cdd:pfam07888 45 ELLQAQEAANRQREKEK---ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1563 knvheleKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFER-DIQAKEEQSEekRRGLVKALRDLEA 1641
Cdd:pfam07888 115 -------EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKaGAQRKEEEAE--RKQLQAKLQQTEE 185
|
..
gi 158285519 1642 EL 1643
Cdd:pfam07888 186 EL 187
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
884-1600 |
2.35e-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: 49.57 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKK---YQQAMEEKTHlAEQLQAEIELCAEAEEGR-ARLVARKQELE 959
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqYQQAVQALEK-ARALCGLPDLTPENAEDYlAAFRAKEQQAT 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 960 ELMQDLESRIEEEEERVNALtSEKKKLQINIQDLEEQLEEEEAAR--------QKLQLEKV-QLDAKLKKMEedvalied 1030
Cdd:COG3096 455 EEVLELEQKLSVADAARRQF-EKAYELVCKIAGEVERSQAWQTARellrryrsQQALAQRLqQLRAQLAELE-------- 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1031 qnhKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERL-------------LKDHQQRQEADRSK-- 1095
Cdd:COG3096 526 ---QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqrselrqqLEQLRARIKELAARap 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1096 --RKIETEVADLKEQINER---RMQIEEMQQQLVKREEELAQtlvridEESAAKAAAQKTQRELE--SQ----------- 1157
Cdd:COG3096 603 awLAAQDALERLREQSGEAladSQEVTAAMQQLLEREREATV------ERDELAARKQALESQIErlSQpggaedprlla 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1158 ---------LAEIQEDLEAEKL---------AR--------SKAEKQKRDLNEELEAL----------------KNELLD 1195
Cdd:COG3096 677 laerlggvlLSEIYDDVTLEDApyfsalygpARhaivvpdlSAVKEQLAGLEDCPEDLyliegdpdsfddsvfdAEELED 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1196 SLDTTAAQQELR------------SKREQEVATLKKTLEDESANHESTLMDmrhkhAQEISSINEQLENLKkmkgglekS 1263
Cdd:COG3096 757 AVVVKLSDRQWRysrfpevplfgrAAREKRLEELRAERDELAEQYAKASFD-----VQKLQRLHQAFSQFV--------G 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1264 KQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVdRVRVELQDKV---------TKLQQESENITQQL 1334
Cdd:COG3096 824 GHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL-KEQLQLLNKLlpqanlladETLADRLEELREEL 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1335 DEAElKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEAlqeqleedeeaktnYEKKLAELNFTIQEM 1414
Cdd:COG3096 903 DAAQ-EAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRR--------------LKQQIFALSEVVQRR 967
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1415 KKRSEEDSdiAKELEESKKkMNkdiETLQRQIQELQAANDRLDKSKKKIQSELEDAT---IELDTQRtkvlelEKKQKNF 1491
Cdd:COG3096 968 PHFSYEDA--VGLLGENSD-LN---EKLRARLEQAEEARREAREQLRQAQAQYSQYNqvlASLKSSR------DAKQQTL 1035
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1492 DKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTREldeafeKIDELETKRKGLQNELDELANTQGTADKNVH----E 1567
Cdd:COG3096 1036 QELEQELEELGVQADAEAEERARIRRDELHEELSQNRS------RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKqereQ 1109
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1568 LEKAK-----------------RALESQLAELKAQ-------------------NEELEDDLQLTEDAK 1600
Cdd:COG3096 1110 VVQAKagwcavlrlardndverRLHRRELAYLSADelrsmsdkalgalrlavadNEHLRDALRLSEDPR 1178
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1285-1596 |
3.05e-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: 48.97 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1285 RQENDRRRKQAETQIAELQV--KLADVDRVRVELQDKVTKLQQESENITQQlDEAELKASaaiksagNLESQLTEAQQLL 1362
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERrrKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERI-------RQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1363 EEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEdsdIAKELEESKKkmnkdiETL 1442
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQ------REV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1443 QRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERdaaEREAREKETK 1522
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER---KQAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1523 VLSLTRELDEAFEKIDELETKRKG-----LQNELDELANTQ-----GTADKNVHELEKAKRALESQLAELKAQNEELEDD 1592
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAeeerrKQQEMEERRRIQeqmrkATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
....
gi 158285519 1593 LQLT 1596
Cdd:pfam17380 595 TPIT 598
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1402-1780 |
3.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1402 KKLAELNFTIQEMKKRSEEDSDIAKELEESKKKmnkdIETLQRQIQELQAANDRLDKSKK--KIQSELEDATIELDTQRT 1479
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEE----LEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1480 KVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAR----EKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELA 1555
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1556 NtQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEV-NMQALRAQ------FERDIQAKEEQSEEK 1628
Cdd:COG4717 227 E-ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIaGVLFLVLGllallfLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1629 RRGLVKALRDLE-AELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKE 1707
Cdd:COG4717 306 ELQALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 1708 ELAAISKESERKVKtLEADLMQLTEDLSS--SERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALE 1780
Cdd:COG4717 386 ELRAALEQAEEYQE-LKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1033-1188 |
3.31e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1033 HKLVKEKKLLEERaNDLSQTLAEEEEKAKHLAKLKvkhestIAELEERLlkdHQQRQEADRSKRKIETEVADLKEQINER 1112
Cdd:PRK12704 25 RKKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEA------LLEAKEEI---HKLRNEFEKELRERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1113 RMQIEEMQQQLVKREEELAQTLVRIDEEsaaKAAAQKTQRELESQLAEIQEDLeaEKLARSKAEKQKRDLNEELEA 1188
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQK---QQELEKKEEELEELIEEQLQEL--ERISGLTAEEAKEILLEKVEE 165
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1427-1743 |
3.59e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.53 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1427 ELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVA 1506
Cdd:pfam19220 59 QERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1507 QERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAK-------RALESQL 1579
Cdd:pfam19220 139 EENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLdatrarlRALEGQL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1580 AELKAQNEELEDDLqLTEDAKLRLEVNMQALR---------------AQFERDIQAKEEQ---SEEKRRGLVKALRDLEA 1641
Cdd:pfam19220 219 AAEQAERERAEAQL-EEAVEAHRAERASLRMKlealtaraaateqllAEARNQLRDRDEAiraAERRLKEASIERDTLER 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1642 ELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKV---KEDALKQAKKLQAQIKDAIrdaeeakaakeelAAISKESER 1718
Cdd:pfam19220 298 RLAGLEADLERRTQQFQEMQRARAELEERAEMLTKAlaaKDAALERAEERIASLSDRI-------------AELTKRFEV 364
|
330 340
....*....|....*....|....*
gi 158285519 1719 KVKTLEADLMQLTEDLsSSERARRA 1743
Cdd:pfam19220 365 ERAALEQANRRLKEEL-QRERAERA 388
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1444-1752 |
3.59e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.53 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1444 RQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKvleLEKKQKNFDKVLAEEKAISEQ---VAQERDAAEREAREKE 1520
Cdd:pfam19220 20 EDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEAL---LAQERAAYGKLRRELAGLTRRlsaAEGELEELVARLAKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1521 TKVLSLTRELDEAFEKIDELETKRKGLQNELD-ELANTQGTADKNVHELEKAKrALESQLAELKAQNEELEDDLQLTEDA 1599
Cdd:pfam19220 97 AALREAEAAKEELRIELRDKTAQAEALERQLAaETEQNRALEEENKALREEAQ-AAEKALQRAEGELATARERLALLEQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1600 KLRLEVNMQALRAQFERdIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKE 1679
Cdd:pfam19220 176 NRRLQALSEEQAAELAE-LTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALT 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1680 DALKQAKKLQAQIKDAIRDAEEAKAA---KEELAAISKES-ERKVKTLEADLMQLTEDLSSSERARRAAEgERDELL 1752
Cdd:pfam19220 255 ARAAATEQLLAEARNQLRDRDEAIRAaerRLKEASIERDTlERRLAGLEADLERRTQQFQEMQRARAELE-ERAEML 330
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
912-1273 |
3.61e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.13 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 912 NSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDLESRIEEEeeRVNALTSEKKKLQINIQ 991
Cdd:PLN02939 43 SSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQ--RDEAIAAIDNEQQTNSK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 992 DLEEQLEeeeaarqkLQLEkvQLDAKLKKMEEDVALIE-------DQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLA 1064
Cdd:PLN02939 121 DGEQLSD--------FQLE--DLVGMIQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1065 KLKVkHESTIAELEERLLKDHQQRQEADRS-KRKIETEVADLKEQINERRMQIEEMQQQLVkreeELAQTLVRIDEESAA 1143
Cdd:PLN02939 191 QEKI-HVEILEEQLEKLRNELLIRGATEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELI----EVAETEERVFKLEKE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1144 KAAAQKTQRELESQLAEIQEDLeaEKLARSKAE---KQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKT 1220
Cdd:PLN02939 266 RSLLDASLRELESKFIVAQEDV--SKLSPLQYDcwwEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEA 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1221 LEDESANHESTLMDMRHKHAQE----------------ISSINEQLENLKKMKgglEKSKQQLEAENAD 1273
Cdd:PLN02939 344 NVSKFSSYKVELLQQKLKLLEErlqasdheihsyiqlyQESIKEFQDTLSKLK---EESKKRSLEHPAD 409
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
894-1338 |
6.74e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.98 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 894 QKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDLESRIEEEE 973
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 974 ERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLV-KEKKLLEERANDLSQT 1052
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAAlAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1053 LAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQ 1132
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1133 TLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQ 1212
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1213 EVATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRR 1292
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 158285519 1293 KQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAE 1338
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1054-1413 |
6.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1054 AEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQT 1133
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1134 LVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQE 1213
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1214 VATLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRK 1293
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1294 QAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALS 1373
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 158285519 1374 SKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQE 1413
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1324-1630 |
7.47e-05 |
|
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: 47.81 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1324 QQESENITQQLDEAELKASAAIKSAGN-LESQLTEAQQLLEEETRQKLALSSKLRQI---ESEKE-ALQEQLEEDEEAKT 1398
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIeLEKKASALKRQLDRESDRNQELQKRIRLLekrEAEAEeALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1399 NYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQ------SELEDATI 1472
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASeaeqlrQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1473 ELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERD-AAEREAREKETKVLSLTRE------------------LDEA 1533
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPElEKELERLREHNKHLNENIEnklllkeevedlkrklerEEKY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1534 FEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAE---LKAQNEELEDDLQLTEDAKLRLEVNMQAL 1610
Cdd:pfam05557 244 REEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQY 323
|
330 340
....*....|....*....|
gi 158285519 1611 RAQFERDIQAKEEQSEEKRR 1630
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRR 343
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
883-1130 |
8.27e-05 |
|
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: 47.73 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 883 LEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQaMEEKTHlaeQLQAEIELCAEAEEGRARLVARKQELEELM 962
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH-LKSKTN---ELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 963 QDLESRIEEEEERVNALTSEKKKLQI-NIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKkl 1041
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQeKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK-- 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1042 lEERANDLSQTLAEEEEKAKHLAK--LKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINErrMQIEEM 1119
Cdd:TIGR00606 976 -ETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQ--MQVLQM 1052
|
250
....*....|.
gi 158285519 1120 QQQLVKREEEL 1130
Cdd:TIGR00606 1053 KQEHQKLEENI 1063
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
883-1135 |
8.68e-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: 47.81 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 883 LEVTKQEEKLVQKEDELRQIRDKLENLSKNS---QEYE--KKYQQAMEEKTHLAEQLQAEIE-LCAEAEEGRarlvarkq 956
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELERLQMERQQKNErvrQELEaaRKVKILEEERQRKIQQQKVEMEqIRAEQEEAR-------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 957 elEELMQDLESRIEEEEERVNALTSEKKKlqiniQDLEEQLEEEEAARQKLQLEKVQldaklkkmeEDVALIEDQNHKLV 1036
Cdd:pfam17380 434 --QREVRRLEEERAREMERVRLEEQERQQ-----QVERLRQQEEERKRKKLELEKEK---------RDRKRAEEQRRKIL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1037 KEKklLEERandlSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKietEVADLKEQINERRMQI 1116
Cdd:pfam17380 498 EKE--LEER----KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR---RIQEQMRKATEERSRL 568
|
250
....*....|....*....
gi 158285519 1117 EEMQqqlvkREEELAQTLV 1135
Cdd:pfam17380 569 EAME-----REREMMRQIV 582
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1117-1287 |
8.96e-05 |
|
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: 46.07 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1117 EEMQQQLVkreeELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDS 1196
Cdd:COG1579 3 PEDLRALL----DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1197 ldtTAAQQELRSKRE-----QEVATLKK---TLEDEsanhESTLMDMRHKHAQEISSINEQLENLKKmkgGLEKSKQQLE 1268
Cdd:COG1579 79 ---EEQLGNVRNNKEyealqKEIESLKRrisDLEDE----ILELMERIEELEEELAELEAELAELEA---ELEEKKAELD 148
|
170
....*....|....*....
gi 158285519 1269 AENADLATELRNVNQSRQE 1287
Cdd:COG1579 149 EELAELEAELEELEAEREE 167
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
948-1167 |
9.58e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 948 RARLVARKQELEELMQDLESRIEEEEERVNAltSEKK----KLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEE 1023
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE--AEAAleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1024 DVALIEDQNhklvkekKLLEERANDLSQTLAEEEEKAKhLAKLkvkhESTIAELEERLLKDHQQRQEADRSKRKIETEva 1103
Cdd:COG3206 241 RLAALRAQL-------GSGPDALPELLQSPVIQQLRAQ-LAEL----EAELAELSARYTPNHPDVIALRAQIAALRAQ-- 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1104 dLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEA 1167
Cdd:COG3206 307 -LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1309-1548 |
9.99e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1309 VDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAG--NLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEAL 1386
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1387 QEQLEEDEEAKT---------NYEKKLAELNFTIQEMKKRSEEDsdiakeleeskkkmNKDIETLQRQIQELqaandrld 1457
Cdd:COG3206 246 RAQLGSGPDALPellqspviqQLRAQLAELEAELAELSARYTPN--------------HPDVIALRAQIAAL-------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1458 ksKKKIQSELEDATIELDTQRtKVLElekkqknfdkvlAEEKAISEQVAQERDAAeREAREKETKVLSLTRELDEAFEKI 1537
Cdd:COG3206 304 --RAQLQQEAQRILASLEAEL-EALQ------------AREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELY 367
|
250
....*....|.
gi 158285519 1538 DELETKRKGLQ 1548
Cdd:COG3206 368 ESLLQRLEEAR 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1004-1645 |
1.33e-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: 47.25 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1004 RQKLQLEKVQLDAKLKKMEEDVALIEdqnhkLVKEKKLLEERANDLSQtlaEEEEKAKHLAKLK--VKHESTIA------ 1075
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVE-----MARELEELSARESDLEQ---DYQAASDHLNLVQtaLRQQEKIEryqedl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1076 -ELEERLLKDHQQRQEADRS-------KRKIETEVADLKEQINERRMQIEEMQ------QQLVKREEElAQTLVRIDEES 1141
Cdd:COG3096 357 eELTERLEEQEEVVEEAAEQlaeaearLEAAEEEVDSLKSQLADYQQALDVQQtraiqyQQAVQALEK-ARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1142 AAKAaaQKTQRELESQLAEI-QEDLEAE-KLARSKAEKQKRDlnEELEALKNeLLDSLDTTAA----QQELRSKREQE-- 1213
Cdd:COG3096 436 PENA--EDYLAAFRAKEQQAtEEVLELEqKLSVADAARRQFE--KAYELVCK-IAGEVERSQAwqtaRELLRRYRSQQal 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1214 ---VATLKKTLED------ESANHESTLMDMRHKHAQEISSiNEQLENLKkmkgglekskQQLEAENADLATELRNVNQS 1284
Cdd:COG3096 511 aqrLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDA-AEELEELL----------AELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1285 RQENDRRRKQAETQIAELqvklADVDRVRVELQDKVTKLQQESENI---TQQLDEAELKASAAIKSAGNLESQLTEAQQL 1361
Cdd:COG3096 580 RSELRQQLEQLRARIKEL----AARAPAWLAAQDALERLREQSGEAladSQEVTAAMQQLLEREREATVERDELAARKQA 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1362 LEEETRQKLALS----SKLRQIeseKEALQEQLEEDEeaktnYE------------------------------KKLAEL 1407
Cdd:COG3096 656 LESQIERLSQPGgaedPRLLAL---AERLGGVLLSEI-----YDdvtledapyfsalygparhaivvpdlsavkEQLAGL 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1408 N--------------------FTIQEMK-----------------------------KRSEEDSDIAKELEESKKKMNKD 1438
Cdd:COG3096 728 EdcpedlyliegdpdsfddsvFDAEELEdavvvklsdrqwrysrfpevplfgraareKRLEELRAERDELAEQYAKASFD 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1439 IETLQRQIQ--------------------ELQAANDRLdkskKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEE 1498
Cdd:COG3096 808 VQKLQRLHQafsqfvgghlavafapdpeaELAALRQRR----SELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQA 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1499 KAISEQVAQERdaaEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALES- 1577
Cdd:COG3096 884 NLLADETLADR---LEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAl 960
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1578 -----------------QLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFErdiQAKEEQSEEKRRGLVKA--LRD 1638
Cdd:COG3096 961 sevvqrrphfsyedavgLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYS---QYNQVLASLKSSRDAKQqtLQE 1037
|
....*..
gi 158285519 1639 LEAELDE 1645
Cdd:COG3096 1038 LEQELEE 1044
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1172 |
1.37e-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: 45.69 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1005 QKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELE-ERLLK 1083
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1084 DHQQRQE-ADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEEsaaKAAAQKTQRELESQLAEIQ 1162
Cdd:COG1579 93 ALQKEIEsLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELA 169
|
170
....*....|
gi 158285519 1163 EDLEAEKLAR 1172
Cdd:COG1579 170 AKIPPELLAL 179
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
924-1303 |
1.50e-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: 47.25 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 924 MEEKTHLAEQLQAEIELCAEAEEgrarLVARKQELEelmQDLESRIEEEEERVNALTSEKK--KLQINIQDLEEQLEEEE 1001
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEE----LSARESDLE---QDYQAASDHLNLVQTALRQQEKieRYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1002 AARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLvkekklleERANDLSQTLA-------EEEEKAKHLAKLKvkhESTI 1074
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADY--------QQALDVQQTRAiqyqqavQALEKARALCGLP---DLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1075 AELEERLLKDHQQRQEADRSKRKIETEVADLKEQIN--ERRMQIEEMQQQLVKREE--ELAQTLVRiDEESAAKAAAQKT 1150
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKAYELVCKIAGEVERSQawQTARELLR-RYRSQQALAQRLQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1151 QreLESQLAEIQEDL----EAEKLARSKAEKQKRDLN---------EELEALKNELLDSLDTTAAQQ-ELRSKREQEVAT 1216
Cdd:COG3096 516 Q--LRAQLAELEQRLrqqqNAERLLEEFCQRIGQQLDaaeeleellAELEAQLEELEEQAAEAVEQRsELRQQLEQLRAR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1217 LKKTLEDESANHEStlmdmrhkhaqeissiNEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAE 1296
Cdd:COG3096 594 IKELAARAPAWLAA----------------QDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALE 657
|
....*..
gi 158285519 1297 TQIAELQ 1303
Cdd:COG3096 658 SQIERLS 664
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
950-1575 |
1.57e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 950 RLVARKQELEELMQDLESRIEEeeerVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIE 1029
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISN----IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1030 DQNHKLVKekklLEERANDLSQTLAEEEEKAKHLAKLKVKhestIAELEERLLKDHQQRQEADRSKRKietEVADLKEQI 1109
Cdd:PRK01156 239 SALNELSS----LEDMKNRYESEIKTAESDLSMELEKNNY----YKELEERHMKIINDPVYKNRNYIN---DYFKYKNDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1110 NERRMQIEEMQQQLVKREEELaQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNE---EL 1186
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAII-KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEyskNI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1187 EALKNELLDSLDTTAAQQELRSKREQEVatlkktledesanhESTLMDMRHKhaqeISSINEQLENLKKMKGGLEKSKQQ 1266
Cdd:PRK01156 387 ERMSAFISEILKIQEIDPDAIKKELNEI--------------NVKLQDISSK----VSSLNQRIRALRENLDELSRNMEM 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1267 LEAEN------ADLATElrNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELK 1340
Cdd:PRK01156 449 LNGQSvcpvcgTTLGEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1341 ASAAIKSAGNLESQLTEAQQLLEEETRQKLALssKLRQIESEkealqeqleedeeaKTNYEKKLAEL-NFTIQEMKKRSe 1419
Cdd:PRK01156 527 ARADLEDIKIKINELKDKHDKYEEIKNRYKSL--KLEDLDSK--------------RTSWLNALAVIsLIDIETNRSRS- 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1420 edsdiakelEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSE---LEDATIELDTQRTKVLELEKKQKNFDKVLA 1496
Cdd:PRK01156 590 ---------NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEannLNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1497 EEKAIseqvaqERDAAEREAR--EKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRA 1574
Cdd:PRK01156 661 EIDSI------IPDLKEITSRinDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
.
gi 158285519 1575 L 1575
Cdd:PRK01156 735 I 735
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1279-1499 |
1.58e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1279 RNVNQSRQENDRRRKQAETQIA------ELQVKLADVDRVRveLQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLE 1352
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKtynkniEEQRKKNGENIAR--KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1353 SQLTEAQQLL-----EEETRQKLALSSK--------LRQIESEKEalqeQLEEDEEAKTNYEKKLAELNFTIQEMKKRSE 1419
Cdd:PHA02562 255 AALNKLNTAAakiksKIEQFQKVIKMYEkggvcptcTQQISEGPD----RITKIKDKLKELQHSLEKLDTAIDELEEIMD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1420 EDSDIAKELEEskkkMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTqrtkvLELEKKQKNFDKV-LAEE 1498
Cdd:PHA02562 331 EFNEQSKKLLE----LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK-----LQDELDKIVKTKSeLVKE 401
|
.
gi 158285519 1499 K 1499
Cdd:PHA02562 402 K 402
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1263-1520 |
1.62e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1263 SKQQLEAENADLATELRNVNQSRQENDR---RRKQAETQIA-------ELQVKLADVDRVRVELQDKVTKLQQ----ESE 1328
Cdd:PRK11637 45 NRDQLKSIQQDIAAKEKSVRQQQQQRASllaQLKKQEEAISqasrklrETQNTLNQLNKQIDELNASIAKLEQqqaaQER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1329 NITQQLDeaelkasAAIKsagnlESQLTEAQQLLEEETRQK----LALSSKLRQIESEkealqeqleedeeaktnyekkl 1404
Cdd:PRK11637 125 LLAAQLD-------AAFR-----QGEHTGLQLILSGEESQRgeriLAYFGYLNQARQE---------------------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1405 aelnfTIQEMKKRSEEDSDIAKELEEsKKKMNKDIETLQRQIQEL--QAANDRldkskKKIQSELEDAtieldtqrtkvl 1482
Cdd:PRK11637 171 -----TIAELKQTREELAAQKAELEE-KQSQQKTLLYEQQAQQQKleQARNER-----KKTLTGLESS------------ 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 158285519 1483 eLEKKQKNFDKVLAEEKAISEQVAQ-ERDA---AEREAREKE 1520
Cdd:PRK11637 228 -LQKDQQQLSELRANESRLRDSIARaEREAkarAEREAREAA 268
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1501-1698 |
1.68e-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: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1501 ISEQVAQERDAAEREAReketkvlSLTRELDEAFEKIDELETKRKGL--QNELDELANTQGTADKNVHELEKAKRALESQ 1578
Cdd:COG3206 162 LEQNLELRREEARKALE-------FLEEQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1579 LAELKAQNEELEDDLQLTEDAKLRLEVN--MQALRAQFerdIQAKEEQSEEKRRGL-----VKALRDLEAELDEERKQRA 1651
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQL---AELEAELAELSARYTpnhpdVIALRAQIAALRAQLQQEA 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158285519 1652 AAVAAKKKLEGD-LKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRD 1698
Cdd:COG3206 312 QRILASLEAELEaLQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
886-1448 |
1.75e-04 |
|
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: 46.66 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 886 TKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQLQaeiELCAEAEEGRARLVARKQELEELMQDL 965
Cdd:pfam05557 65 AEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELS---ELRRQIQRAELELQSTNSELEELQERL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 966 E------SRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLdAKLKKMEEDVALIEDQNHKL---V 1036
Cdd:pfam05557 142 DllkakaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLnenI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1037 KEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERllkdhqqrqeadrsKRKIETEVADLKEQINERRMQI 1116
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSW--------------VKLAQDTGLNLRSPEDLSRRIE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1117 EEMQQQLVKREEELAQTlvrideesAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNE---- 1192
Cdd:pfam05557 287 QLQQREIVLKEENSSLT--------SSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKErdgy 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1193 --LLDSLDTTAAQQELRSKREQEVATLKKTLEDESANHEStlmdMRHKhaqeISSINEQLENLKKMKGGLEKSKQQL--E 1268
Cdd:pfam05557 359 raILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEE----MEAQ----LSVAEEELGGYKQQAQTLERELQALrqQ 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1269 AENADLATELRNVNQSRQENDR---RRKQAETQIAELQVKLAdvdrvRVELQD----KVTKLQQESENITQqldEAElka 1341
Cdd:pfam05557 431 ESLADPSYSKEEVDSLRRKLETlelERQRLREQKNELEMELE-----RRCLQGdydpKKTKVLHLSMNPAA---EAY--- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1342 saaiksagnlESQLTEAQQLLEEETRqklaLSSKLRQIESEKEalqeqleedeeaktnyekKLAELNFTIQEMKKRseED 1421
Cdd:pfam05557 500 ----------QQRKNQLEKLQAEIER----LKRLLKKLEDDLE------------------QVLRLPETTSTMNFK--EV 545
|
570 580
....*....|....*....|....*..
gi 158285519 1422 SDIAKELEESKKKMNKDIETLQRQIQE 1448
Cdd:pfam05557 546 LDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
990-1216 |
1.78e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 990 IQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVK 1069
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1070 HESTIAELEERL----LKDHQQRQEAdrsKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEEsaaka 1145
Cdd:COG3883 98 SGGSVSYLDVLLgsesFSDFLDRLSA---LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1146 aaqktQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVAT 1216
Cdd:COG3883 170 -----KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1351-1539 |
1.82e-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: 45.30 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1351 LESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDiakelee 1430
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1431 skkkmNKDIETLQRQIQELqaandrldkskKKIQSELEDATIELDTqrtkvlELEKKQKNFDKVLAEEKAISEQVAQERD 1510
Cdd:COG1579 88 -----NKEYEALQKEIESL-----------KRRISDLEDEILELME------RIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|....*....
gi 158285519 1511 AAEREAREKETKVLSLTRELDEAFEKIDE 1539
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1274-1408 |
2.09e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1274 LATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENItqqLDEAELKASAAIKSAgnles 1353
Cdd:PRK00409 511 IGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKEA----- 582
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1354 QLTEAQQLLEEETRQKLALSS-KLRQIESEKEALQEQLEEDEEAKTNYEKKLAELN 1408
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASvKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1767-1974 |
2.15e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1767 DEKRRLEARIAALEEELEEEQSNLELmvDRNRKAQLTIEQLTTELATEKSNSqnnETLKCGLERLNKELKAKLSEQETAL 1846
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1847 R--TKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNL 1924
Cdd:COG1196 295 AelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 158285519 1925 DEAEEEIQKEKTLKRKAQRECEDMLESHEALSREVNALKSKLSIHKDSKK 1974
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1398-1598 |
2.24e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1398 TNYEKKLAELNFTIQEMKKRSEEDsdIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSeLEDATIEldtq 1477
Cdd:PRK05771 63 RSYLPKLNPLREEKKKVSVKSLEE--LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEP-WGNFDLD---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1478 rtkvLELEKKQKN---FDKVLAEEKAISEQVAQERDAAEREAREKETK---VLSLTRELDEAFEKIDELETKRKGLQNEl 1551
Cdd:PRK05771 136 ----LSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvvVVVLKELSDEVEEELKKLGFERLELEEE- 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1552 delantqGTADKNVHELEKAKRALESQL----AELKAQNEELEDDLQLTED 1598
Cdd:PRK05771 211 -------GTPSELIREIKEELEEIEKEResllEELKELAKKYLEELLALYE 254
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1321-1606 |
2.47e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1321 TKLQQESENITQQLDEAelkaSAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIES------------EKEALQE 1388
Cdd:NF012221 1538 SESSQQADAVSKHAKQD----DAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLEStdqnaletngqaQRDAILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1389 QLEEDEEAKTNYEKKLAELNFTIQEMKKRSEE---------DSDIAKELEESKKKMNKDIETL-QRQIQELQAANDRLDK 1458
Cdd:NF012221 1614 ESRAVTKELTTLAQGLDALDSQATYAGESGDQwrnpfagglLDRVQEQLDDAKKISGKQLADAkQRHVDNQQKVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1459 SKK-KIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETkvlsltreldeAFEKI 1537
Cdd:NF012221 1694 SEAgVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASA-----------AENKA 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1538 DELETKRKGLQNELDELANTQG----TADKNVHELEKAKRALESQLAELKAQ-----NEEL-EDDLQLTEDAKL---RLE 1604
Cdd:NF012221 1763 NQAQADAKGAKQDESDKPNRQGaagsGLSGKAYSVEGVAEPGSHINPDSPAAadgrfSEGLtEQEQEALEGATNavnRLQ 1842
|
..
gi 158285519 1605 VN 1606
Cdd:NF012221 1843 IN 1844
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1298-1474 |
2.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1298 QIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEetrqklaLSSKLR 1377
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-------YEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1378 QIESEKE--ALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEdsdIAKELEESKKKMNKDIETLQRQIQELQAANDR 1455
Cdd:COG1579 84 NVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAE---LEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|....*....
gi 158285519 1456 LDKSKKKIQSELEDATIEL 1474
Cdd:COG1579 161 LEAEREELAAKIPPELLAL 179
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1363-1650 |
2.77e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1363 EEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETL 1442
Cdd:pfam07888 62 ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1443 QRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQvaqeRDAAEREAREKETK 1522
Cdd:pfam07888 142 TQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQ----RDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1523 vlsLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAEL-KAQNEELEDDLQLTeDAKL 1601
Cdd:pfam07888 218 ---LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELhQARLQAAQLTLQLA-DASL 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 158285519 1602 RLEVNmQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQR 1650
Cdd:pfam07888 294 ALREG-RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
966-1178 |
3.04e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 966 ESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDvalIEDQNHKLVKEKKLLEER 1045
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1046 ANDLSQT---------LAEEEEKAKHLAKLKVKheSTIAELEERLLKDHQQ-RQEADRSKRKIETEVADLKEQINERRMQ 1115
Cdd:COG3883 92 ARALYRSggsvsyldvLLGSESFSDFLDRLSAL--SKIADADADLLEELKAdKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158285519 1116 IEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQ 1178
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PLN03223 |
PLN03223 |
Polycystin cation channel protein; Provisional |
1455-1584 |
3.14e-04 |
|
Polycystin cation channel protein; Provisional
Pssm-ID: 215637 [Multi-domain] Cd Length: 1634 Bit Score: 46.09 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1455 RLDKSKKKIQSELEDATieLDTQRTKVLELEKKQKNFDKVLAEEKaiseqVAQERDAAEREAREKETKVLSL-TRELDE- 1532
Cdd:PLN03223 763 ATRANRRRLQQTNAAAT--LTNILTQVGTLSTTQTSLDTQIETLK-----TQQDRANQEAEAHHADNSLETLiNAGFTDi 835
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1533 -----AFE-KIDELETKRK----GLQNELDELANTQGTADKNVHELEKAKRALESQLAELKA 1584
Cdd:PLN03223 836 kagqaALEaKLDEILGKQQqalaAAQESLAIQQRTNGLAERQAAAIEKLAKAVEKQLSSIKS 897
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
895-1944 |
3.30e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 895 KEDELRQIRDK--LENL-SKNSQEYEKKyqQAMEEKT---HLAEQLQAEIELCAEAEEGRARLVAR-KQELEELMQDLES 967
Cdd:TIGR01612 685 KENAIDNTEDKakLDDLkSKIDKEYDKI--QNMETATvelHLSNIENKKNELLDIIVEIKKHIHGEiNKDLNKILEDFKN 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 968 RIEEEEERVNALTSEKKKLQI---NIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEE 1044
Cdd:TIGR01612 763 KEKELSNKINDYAKEKDELNKyksKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKD 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1045 RAndLSQTLAEEEEKAKHLAKLKVKHEStIAELEERLlkdhqQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLv 1124
Cdd:TIGR01612 843 DF--LNKVDKFINFENNCKEKIDSEHEQ-FAELTNKI-----KAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNI- 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1125 kreeelaQTLVRIDEesaakaaaqktqrelesQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNelldsldTTAAQQ 1204
Cdd:TIGR01612 914 -------NTLKKVDE-----------------YIKICENTKESIEKFHNKQNILKEILNKNIDTIKE-------SNLIEK 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1205 ELRSKREQEVatLKKTLEDESANHESTLMDMRHKHAQEISSINEQLENLKKMKGGL------EKSK------QQLEAENA 1272
Cdd:TIGR01612 963 SYKDKFDNTL--IDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfdEKEKatndieQKIEDANK 1040
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1273 DLA-------TELRNVNQSRQE---------NDRRRKQAETQIAEL-----QVKLADVDRV----RVELQDKVTKLQQES 1327
Cdd:TIGR01612 1041 NIPnieiaihTSIYNIIDEIEKeigkniellNKEILEEAEINITNFneikeKLKHYNFDDFgkeeNIKYADEINKIKDDI 1120
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1328 ENITQQLDEaELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAEL 1407
Cdd:TIGR01612 1121 KNLDQKIDH-HIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEI 1199
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1408 NfTIQEMKKRSEEDSDI------------AKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKK------IQSELED 1469
Cdd:TIGR01612 1200 A-EIEKDKTSLEEVKGInlsygknlgklfLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEmgiemdIKAEMET 1278
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1470 ATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREaREKETKVLSLTR---ELDEAFEKIDELET---- 1542
Cdd:TIGR01612 1279 FNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIK-KELQKNLLDAQKhnsDINLYLNEIANIYNilkl 1357
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1543 -KRKGLQNELDELANTQGTADKNVH-ELEKAKRALE-----SQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAqfE 1615
Cdd:TIGR01612 1358 nKIKKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKkikddINLEECKSKIESTLDDKDIDECIKKIKELKNHILSE--E 1435
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1616 RDIQAKEEQSEEKRRGLVKALRDLE-AELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQA---- 1690
Cdd:TIGR01612 1436 SNIDTYFKNADENNENVLLLFKNIEmADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkel 1515
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1691 --QIKDAIRDAEEAKAAKEELAAISK---ESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLM 1765
Cdd:TIGR01612 1516 feQYKKDVTELLNKYSALAIKNKFAKtkkDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAA 1595
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1766 IDekrrleariaaleeeleeeqsnlelmvdrnrkAQLTIEQLTTELateksnsqnnetLKcgLERLNKELKAKLSEQETa 1845
Cdd:TIGR01612 1596 ID--------------------------------IQLSLENFENKF------------LK--ISDIKKKINDCLKETES- 1628
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1846 LRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRKlekrikeltmNIEDERRHADQYKEQIEKANNRMKTLKRNLD 1925
Cdd:TIGR01612 1629 IEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQKK----------NIEDKKKELDELDSEIEKIEIDVDQHKKNYE 1698
|
1130
....*....|....*....
gi 158285519 1926 EAEEEIQKEKTLKRKAQRE 1944
Cdd:TIGR01612 1699 IGIIEKIKEIAIANKEEIE 1717
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1153-1350 |
3.66e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1153 ELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSldttaaqQELRSKREQEVATLKKTLEDESANHestl 1232
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------EKEIKRLELEIEEVEARIKKYEEQL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1233 mdMRHKHAQEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVnqsrqendrrRKQAETQIAELQVKLADVDRV 1312
Cdd:COG1579 83 --GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAEL----------EAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 158285519 1313 RVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGN 1350
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPPELLALYERIRKRKN 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
942-1173 |
3.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 942 AEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEeqlEEEEAARQKLQLEKVQLDAKLKKM 1021
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1022 EEDVALIEDQNHKLVKEKKLLE--------ERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADR 1093
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1094 SKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARS 1173
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1540-1693 |
4.26e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1540 LET-KRKGLQNELDELANTQGTADKNvhELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDI 1618
Cdd:PRK00409 491 FEIaKRLGLPENIIEEAKKLIGEDKE--KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 1619 QAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAakkklEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIK 1693
Cdd:PRK00409 569 EEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK-----AHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1332-1585 |
4.64e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1332 QQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKlalSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTI 1411
Cdd:PLN02939 39 RRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLE---NTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1412 QEMKKRSEEDSDIA-KELEESKKKMNKDIETL-QRQIQELQAANdrldkskkKIQSELEDATIELDTQRTKVLELEKKQK 1489
Cdd:PLN02939 116 QTNSKDGEQLSDFQlEDLVGMIQNAEKNILLLnQARLQALEDLE--------KILTEKEALQGKINILEMRLSETDARIK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1490 NFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTqgtaDKNVHELE 1569
Cdd:PLN02939 188 LAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET----EERVFKLE 263
|
250
....*....|....*.
gi 158285519 1570 KAKRALESQLAELKAQ 1585
Cdd:PLN02939 264 KERSLLDASLRELESK 279
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1403-1636 |
4.86e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1403 KLAELNFTIQ--EMKKRS-EEDSDIAKELEESKKKMNKD--------IETLQRQIQELQAANDRLDKSKKKIQSELEDAT 1471
Cdd:PHA02562 175 KIRELNQQIQtlDMKIDHiQQQIKTYNKNIEEQRKKNGEniarkqnkYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1472 IELDTQRTKVLELEKKQKNFDKVLA--EEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELEtkrkGLQN 1549
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE----EIMD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1550 ELDELAntqgtadKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEK- 1628
Cdd:PHA02562 331 EFNEQS-------KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKy 403
|
....*...
gi 158285519 1629 RRGLVKAL 1636
Cdd:PHA02562 404 HRGIVTDL 411
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1250-1550 |
4.93e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.42 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1250 LENLKKMKGGLEKSKQQLEAENadlatELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESEN 1329
Cdd:pfam15905 59 LELKKKSQKNLKESKDQKELEK-----EIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1330 ITQQLDEAELKASaaiksagnlesqlteaqqllEEETRQKL-ALSSKLRQIESEKEALQEQLEEDEEaktNYEKKLAELN 1408
Cdd:pfam15905 134 LTRVNELLKAKFS--------------------EDGTQKKMsSLSMELMKLRNKLEAKMKEVMAKQE---GMEGKLQVTQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1409 FTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQ 1488
Cdd:pfam15905 191 KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKE 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1489 KNFDKVLAEEKAISEQVAQERDAAEREAREKEtkvLSLTRELDEAFEKIDELETKRKGLQNE 1550
Cdd:pfam15905 271 QELSKQIKDLNEKCKLLESEKEELLREYEEKE---QTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
879-1193 |
5.12e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 879 VKPLLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQE------------------YEKKYQQAMEEKTHLAEQLQAEIEL 940
Cdd:pfam01576 797 VKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKklknleaellqlqedlaaSERARRQAQQERDELADEIASGASG 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 941 CAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKK 1020
Cdd:pfam01576 877 KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1021 MEEDValiedqnhklvkekklleerandlsqtlaeeeeKAKHLAKLKVKhESTIAELEERLLKDHQQRQEADRSKRKIET 1100
Cdd:pfam01576 957 MEGTV---------------------------------KSKFKSSIAAL-EAKIAQLEEQLEQESRERQAANKLVRRTEK 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1101 EVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQEDLEAeklarskaekqkr 1180
Cdd:pfam01576 1003 KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNES------------- 1069
|
330
....*....|...
gi 158285519 1181 dLNEELEALKNEL 1193
Cdd:pfam01576 1070 -MNREVSTLKSKL 1081
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1148-1385 |
5.31e-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: 44.28 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1148 QKTQRELESQLAEIQEDLEAEKLARSKAEKQ--KRDLNEELEALKNELLD-SLDTTAAQQELRsKREQEVATLKKTLEDE 1224
Cdd:cd22656 83 QNAGGTIDSYYAEILELIDDLADATDDEELEeaKKTIKALLDDLLKEAKKyQDKAAKVVDKLT-DFENQTEKDQTALETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1225 SANHESTLMDmrhkhaqeissineqlENLKKMKGGLEKSKQQLEAENADLATELRNvnqsrqendrRRKQAETQIAELQV 1304
Cdd:cd22656 162 EKALKDLLTD----------------EGGAIARKEIKDLQKELEKLNEEYAAKLKA----------KIDELKALIADDEA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1305 KLADVDRvrveLQDKVTKLQQESENITQQLDEAeLKASAAIKSA-GNLESQLTEAQQLLEEETRQKLALSSKLRQIESEK 1383
Cdd:cd22656 216 KLAAALR----LIADLTAADTDLDNLLALIGPA-IPALEKLQGAwQAIATDLDSLKDLLEDDISKIPAAILAKLELEKAI 290
|
..
gi 158285519 1384 EA 1385
Cdd:cd22656 291 EK 292
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
884-1061 |
6.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 884 EVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEkthlAEQLQAEIE-LCAEAEEGRARLVARKQELEELM 962
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE----LEALQAEIDkLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 963 QD--------------LESR---------------IEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQ 1013
Cdd:COG3883 93 RAlyrsggsvsyldvlLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158285519 1014 LDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAK 1061
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1433-1777 |
6.35e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.04 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1433 KKMNKDIETLQRQIQELQA-ANDRLDKSKKKIQSELEdatiELDTQR-TKVLELEKKQKNFDKVLAEEKAISEQVAQERD 1510
Cdd:PTZ00108 1002 GKLERELARLSNKVRFIKHvINGELVITNAKKKDLVK----ELKKLGyVRFKDIIKKKSEKITAEEEEGAEEDDEADDED 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1511 AAEREAREKE------TKVLSLTREldeafeKIDELETKRKGLQNELDELANTQgTADKNVHELEKAKRALESQlaELKA 1584
Cdd:PTZ00108 1078 DEEELGAAVSydyllsMPIWSLTKE------KVEKLNAELEKKEKELEKLKNTT-PKDMWLEDLDKFEEALEEQ--EEVE 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1585 QNEELEdDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRaaAVAAKKKLEGDL 1664
Cdd:PTZ00108 1149 EKEIAK-EQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKP--DNKKSNSSGSDQ 1225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1665 KDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDL----SSSERA 1740
Cdd:PTZ00108 1226 EDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGEsnggSKPSSP 1305
|
330 340 350
....*....|....*....|....*....|....*..
gi 158285519 1741 RRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIA 1777
Cdd:PTZ00108 1306 TKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVK 1342
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1528-1650 |
6.37e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1528 RELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAK----LRL 1603
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyeaLQK 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1604 EVNMQALRAQF----ERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQR 1650
Cdd:COG1579 97 EIESLKRRISDledeILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
881-1215 |
6.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 881 PLLEVTKQEEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEE-KTHLAEQLQAEIElcAEAEEGRARLVARKQELE 959
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFiGSHLAVAFEADPE--AELRQLNRRRVELERALA 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 960 EL---MQDLESRIEEEEERVNALtsEKKKLQINIQDLEEQLEEEEAARQKL------------------QLEKVQldAKL 1018
Cdd:PRK04863 855 DHesqEQQQRSQLEQAKEGLSAL--NRLLPRLNLLADETLADRVEEIREQLdeaeeakrfvqqhgnalaQLEPIV--SVL 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1019 KKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEE-----EEKAKHLAKlkvkhESTIAE-LEERLLKDHQQRQEAD 1092
Cdd:PRK04863 931 QSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAK-----NSDLNEkLRQRLEQAEQERTRAR 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1093 RSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTqrelesqlaEIQEDLEAEKLAR 1172
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRD---------ELHARLSANRSRR 1076
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 158285519 1173 SKAEKQKRDLNEELEALKNELldsldtTAAQQELRSKREQEVA 1215
Cdd:PRK04863 1077 NQLEKQLTFCEAEMDNLTKKL------RKLERDYHEMREQVVN 1113
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1241-1553 |
6.68e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1241 QEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKV 1320
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1321 TKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSsklrQIESEKEALQEQLEEDEEAKTNY 1400
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS----EAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1401 EKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTK 1480
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158285519 1481 VLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDE 1553
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1503-1746 |
6.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1503 EQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANtqgtadknvhELEKAKRALESQLAEL 1582
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1583 KAQNEeledDLQLTEDAKLRLEV------------NMQALRAQFERD-------------IQAKEEQSEEKRRGLVKALR 1637
Cdd:COG3883 89 GERAR----ALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADadlleelkadkaeLEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1638 DLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESE 1717
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260
....*....|....*....|....*....
gi 158285519 1718 RKVKTLEADLMQLTEDLSSSERARRAAEG 1746
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1242-1385 |
6.97e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1242 EISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDrvrvELQDKVT 1321
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE----EQLGNVR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1322 K------LQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEA 1385
Cdd:COG1579 87 NnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1437-1698 |
7.29e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1437 KDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLaeekaiseqvaqerDAAEREA 1516
Cdd:pfam00038 54 KEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDL--------------DEATLAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1517 REKETKVLSLTreldeafekiDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQL- 1595
Cdd:pfam00038 120 VDLEAKIESLK----------EELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREe 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1596 --------TEDAKLRLEVNMQALRaqferdiQAKEEQSEEKRRglvkaLRDLEAELDEERKQRaaavaakKKLEGDLKDM 1667
Cdd:pfam00038 190 aeewyqskLEELQQAAARNGDALR-------SAKEEITELRRT-----IQSLEIELQSLKKQK-------ASLERQLAET 250
|
250 260 270
....*....|....*....|....*....|.
gi 158285519 1668 EATLEMnnkvkedALKQAKKLQAQIKDAIRD 1698
Cdd:pfam00038 251 EERYEL-------QLADYQELISELEAELQE 274
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
978-1649 |
8.03e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 978 ALTSEKKKL---QINIQDLEE---QLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEdqnhklvkekklLEERANDLSQ 1051
Cdd:PRK10246 227 VLTDEEKQLltaQQQQQQSLNwltRLDELQQEASRRQQALQQALAAEEKAQPQLAALS------------LAQPARQLRP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1052 TLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRmQIEEMQQQLVKREEELA 1131
Cdd:PRK10246 295 HWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHD-RFRQWNNELAGWRAQFS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1132 QTLVRIDEESAAKAAAQKTQRELESqLAEIQEDLEAEKLARSKAEK-QKRDLNEELEALKNELLDSLDTTAAQQELRSKR 1210
Cdd:PRK10246 374 QQTSDREQLRQWQQQLTHAEQKLNA-LPAITLTLTADEVAAALAQHaEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1211 EQEVATLKKTLEDESANHEStlmdmRHKHAQEISSINEQLENLKKmkggLEKSKQQLEAENADL---ATELRNVNQSR-- 1285
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKE-----KTQQLADVKTICEQEARIKD----LEAQRAQLQAGQPCPlcgSTSHPAVEAYQal 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1286 --QENDRRRKQAETQIAELQVK----LADVDRVRVELQ---DKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLT 1356
Cdd:PRK10246 524 epGVNQSRLDALEKEVKKLGEEgaalRGQLDALTKQLQrdeSEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1357 EA----QQLleEETRQKLALSSklrQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEmkkRSEEDSDIAKELEESK 1432
Cdd:PRK10246 604 AQeeheRQL--RLLSQRHELQG---QIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQ---EDEEASWLATRQQEAQ 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1433 KKMNKDIE--TLQRQIQELQAANDRLDKSKkkiQSELEDATIELDTQR---TKVLELEKKQKNFDKVLAEEKAISEQVAQ 1507
Cdd:PRK10246 676 SWQQRQNEltALQNRIQQLTPLLETLPQSD---DLPHSEETVALDNWRqvhEQCLSLHSQLQTLQQQDVLEAQRLQKAQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1508 ERDAAeREAREKETKVLSLTRELDEafEKIDELETKRKGLQNELDelantQGTAdknvhELEKAKRALESQLaelkAQNE 1587
Cdd:PRK10246 753 QFDTA-LQASVFDDQQAFLAALLDE--ETLTQLEQLKQNLENQRQ-----QAQT-----LVTQTAQALAQHQ----QHRP 815
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158285519 1588 ELEDDLQLTEDAKLRLEVNMQALRAQFER--DIQAKEEQSEEKRrglvKALRDLEAELDEERKQ 1649
Cdd:PRK10246 816 DGLDLTVTVEQIQQELAQLAQQLRENTTRqgEIRQQLKQDADNR----QQQQALMQQIAQATQQ 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
956-1118 |
8.13e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 956 QELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQN--H 1033
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1034 KLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEAdrsKRKIETEVADLKEQINERR 1113
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELA 169
|
....*
gi 158285519 1114 MQIEE 1118
Cdd:COG1579 170 AKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1374-1630 |
1.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1374 SKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMK-------KRSEEDSDIAKELEESKKKMNKDIETLQRQI 1446
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAekrdelnAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1447 QELQAANDRLDK---SKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQ--ERDAAEREAREKET 1521
Cdd:COG1340 81 DELNEKLNELREeldELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKEleKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1522 KVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKL 1601
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|....*....
gi 158285519 1602 RLEVNMQALRAQFERDIQAKEEQSEEKRR 1630
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
924-1184 |
1.09e-03 |
|
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: 43.73 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 924 MEEKTHLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLeeeeaa 1003
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1004 rQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLK 1083
Cdd:pfam07888 83 -AELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1084 DHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLAEIQE 1163
Cdd:pfam07888 162 AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS 241
|
250 260
....*....|....*....|.
gi 158285519 1164 DLEAEKLARSKAEKQKRDLNE 1184
Cdd:pfam07888 242 LQERLNASERKVEGLGEELSS 262
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1507-1605 |
1.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1507 QERDAAEREAREKETKVLSLTRELDEA-FEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQ---LAEL 1582
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRygkIPEL 490
|
90 100
....*....|....*....|...
gi 158285519 1583 KAQNEELEDDLQlTEDAKLRLEV 1605
Cdd:COG0542 491 EKELAELEEELA-ELAPLLREEV 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1942 |
1.16e-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: 43.60 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1714 KESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLELM 1793
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1794 VdrnRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQETALrTKLKAATAASEAKNLNLEKQLENETK 1873
Cdd:COG4942 110 L---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1874 ERLAVQKANRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRKAQ 1942
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1012-1965 |
1.17e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1012 VQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSqtlaEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEA 1091
Cdd:TIGR01612 575 IHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNIS----DKNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEH 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1092 DRSKRKIETEVADLKEQINERRMqieemqqqlvkreEELAQTLVRIDEESAAKAAAQKTQRE-LESQLaeiqeDLEAEKL 1170
Cdd:TIGR01612 651 LKNKDKIYSTIKSELSKIYEDDI-------------DALYNELSSIVKENAIDNTEDKAKLDdLKSKI-----DKEYDKI 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1171 ARSKAEKQKRDLNEeLEALKNELLDSLdttaaqQELRSKREQEVAT-LKKTLED---------ESANHESTLMDMRHKHA 1240
Cdd:TIGR01612 713 QNMETATVELHLSN-IENKKNELLDII------VEIKKHIHGEINKdLNKILEDfknkekelsNKINDYAKEKDELNKYK 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1241 QEISSINEQ------LENLKK--MKGGLEKSKQQL------EAENADLATELRNVNQS---------RQENDRRRK--QA 1295
Cdd:TIGR01612 786 SKISEIKNHyndqinIDNIKDedAKQNYDKSKEYIktisikEDEIFKIINEMKFMKDDflnkvdkfiNFENNCKEKidSE 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1296 ETQIAELqvkladVDRVRVELQDKVTKLQQESENITQQLD-------EAELKASAAIKSAGNLESQLTEAQQLLEEETRQ 1368
Cdd:TIGR01612 866 HEQFAEL------TNKIKAEISDDKLNDYEKKFNDSKSLIneinksiEEEYQNINTLKKVDEYIKICENTKESIEKFHNK 939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1369 KLALSSKLRQ-IESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEE--DSDIAKELEESKKKMNKDIE-TLQR 1444
Cdd:TIGR01612 940 QNILKEILNKnIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEakNNELIKYFNDLKANLGKNKEnMLYH 1019
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1445 QIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLElekkqknfdkvlaeekAISEQVAQERDAAEREAREKETKVL 1524
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIID----------------EIEKEIGKNIELLNKEILEEAEINI 1083
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1525 SLTRELDEAFEKIDELETKRKG---LQNEL----DELANTQGTADKNVHELEKAKRALESQLAELKAQNEELED--DLQL 1595
Cdd:TIGR01612 1084 TNFNEIKEKLKHYNFDDFGKEEnikYADEInkikDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvaDKAI 1163
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1596 TEDAKLRLEVNMQALRAQFERDIQ---------------AKEEQSEEKRRGLV----KALRDLEAE-LDEERKQRaaava 1655
Cdd:TIGR01612 1164 SNDDPEEIEKKIENIVTKIDKKKNiydeikkllneiaeiEKDKTSLEEVKGINlsygKNLGKLFLEkIDEEKKKS----- 1238
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1656 akkklEGDLKDMEATLEMNNKVKEDA--LKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTED 1733
Cdd:TIGR01612 1239 -----EHMIKAMEAYIEDLDEIKEKSpeIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIED 1313
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1734 LSSSERARRAAEGERDELLEEINSNSSKGSLM--------IDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIE 1805
Cdd:TIGR01612 1314 FSEESDINDIKKELQKNLLDAQKHNSDINLYLneianiynILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIK 1393
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1806 QLTTELATEKSNSQNNETLKC----GLERLNKELKAKLSEQETALRTKLKAATAASEAKNLNLE--KQLENETKERLAVQ 1879
Cdd:TIGR01612 1394 KIKDDINLEECKSKIESTLDDkdidECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKniEMADNKSQHILKIK 1473
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1880 KANrklekrikeltmNIEDERRHADQYKEQIEKANNrmktLKRNLDEAEEEIQKEKTLKRKAQRECEDMLESHEALSREV 1959
Cdd:TIGR01612 1474 KDN------------ATNDHDFNINELKEHIDKSKG----CKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKN 1537
|
....*.
gi 158285519 1960 NALKSK 1965
Cdd:TIGR01612 1538 KFAKTK 1543
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
892-1224 |
1.23e-03 |
|
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: 43.94 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 892 LVQKEDELRQIRDKLENLSKNSQEYEKkyqQAMEEKTHLAEQLQAEIELCAEAEegraRLVARKQELEELMQDLESRIEE 971
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLK---EVEDLKTELEKEKLKNIELTAHCD----KLLLENKELTQEASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 972 EEERVNALTSEKKKLQINIQDLEEQLE----EEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERAN 1047
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1048 DLSQTLAEEEEKAKHLAK----LKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQl 1123
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQenkaLKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE- 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1124 VKREEELAQTLVRIDEE---------SAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELL 1194
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEidkrcqhkiAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELL 756
|
330 340 350
....*....|....*....|....*....|
gi 158285519 1195 DSLDTTAAQQELRSKREQEVATLKKTLEDE 1224
Cdd:pfam05483 757 SLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
889-1122 |
1.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 889 EEKLVQKEDELRQIRDKLENLSKNSQEYEKKYQQAMEEKTHLAEQL---QAEIE-LCAEAEEGRARLVARKQELEELMQD 964
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELealQAEIDkLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 965 LeSRIEEEEERVNALTSEKkklqiNIQDleeqleeeeAARQKLQLEKVqldaklkkMEEDVALIEDQNH---KLVKEKKL 1041
Cdd:COG3883 95 L-YRSGGSVSYLDVLLGSE-----SFSD---------FLDRLSALSKI--------ADADADLLEELKAdkaELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1042 LEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQ 1121
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
.
gi 158285519 1122 Q 1122
Cdd:COG3883 232 A 232
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1797-1974 |
1.35e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1797 NRKAQLTIE-QLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQETALRtkLKAATAASEAKNLNLEKQLENETKER 1875
Cdd:COG5022 819 IIKLQKTIKrEKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIY--LQSAQRVELAERQLQELKIDVKSISS 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1876 LAVQkaNRKLEKRIKELTMNIEDERRhadqykEQIEKANNRMKTLKRNLDEAE---------------EEIQKEKTLKRK 1940
Cdd:COG5022 897 LKLV--NLELESEIIELKKSLSSDLI------ENLEFKTELIARLKKLLNNIDleegpsieyvklpelNKLHEVESKLKE 968
|
170 180 190
....*....|....*....|....*....|....
gi 158285519 1941 AQRECEDMLESHEALSREVNALKSKLSIHKDSKK 1974
Cdd:COG5022 969 TSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1472-1967 |
1.38e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1472 IELDTQRtKVLELEKKQkNFDKVLAEekaISEQVA--QERDAAEREAREKET-----KVLSLTRELDE-AFEKIDELETK 1543
Cdd:pfam15921 59 VELDSPR-KIIAYPGKE-HIERVLEE---YSHQVKdlQRRLNESNELHEKQKfylrqSVIDLQTKLQEmQMERDAMADIR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1544 RKGLQNELDELANTQGTadknVHELEKAKRALESQLAELKAQNEELEDdLQLTEDAKLRlevNMQALRAQFE----RDIQ 1619
Cdd:pfam15921 134 RRESQSQEDLRNQLQNT----VHELEAAKCLKEDMLEDSNTQIEQLRK-MMLSHEGVLQ---EIRSILVDFEeasgKKIY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1620 AKEEQSEEKRRGLVKALRDLEAELDEErkqraaavaaKKKLEGDLKDMEATLEmnnKVKEDALKQAKKLQAQIKDAIrda 1699
Cdd:pfam15921 206 EHDSMSTMHFRSLGSAISKILRELDTE----------ISYLKGRIFPVEDQLE---ALKSESQNKIELLLQQHQDRI--- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1700 eeakaakeelaaiskesERKVKTLEADLMQLTEDlSSSERARRAAEGERDELLEEINSNssKGSLMIDEKRRLEAriaal 1779
Cdd:pfam15921 270 -----------------EQLISEHEVEITGLTEK-ASSARSQANSIQSQLEIIQEQARN--QNSMYMRQLSDLES----- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1780 eeeleeeqsnlelmvdrnrkaqlTIEQLTTELATEKSNSQNNetlkcgLERLNKELKAKLSEQeTALRTKLKAATAASEa 1859
Cdd:pfam15921 325 -----------------------TVSQLRSELREAKRMYEDK------IEELEKQLVLANSEL-TEARTERDQFSQESG- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1860 knlNLEKQLenetkerlavQKANRKLEKRIKELTMNIEDERRHADQykeqiEKANN-RMKTLKRNLDEAEEEIQKEKTLK 1938
Cdd:pfam15921 374 ---NLDDQL----------QKLLADLHKREKELSLEKEQNKRLWDR-----DTGNSiTIDHLRRELDDRNMEVQRLEALL 435
|
490 500
....*....|....*....|....*....
gi 158285519 1939 RKAQRECEDMLESHEALSREVNALKSKLS 1967
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLEKVS 464
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1205-1627 |
1.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1205 ELRSKREQEVATLKKTLEDEsanhESTLMDMRhkhaqeissinEQLENLKKMKGGLEkskQQLEAENADLAtelRNVNQS 1284
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAE----QYRLVEMA-----------RELAELNEAESDLE---QDYQAASDHLN---LVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1285 RQENDRRRKQAEtqIAELQVKLadvdrvrvELQDKVTKLQQEsenitqQLDEAELKASAAIKSAGNLESQLTEAQQLLEE 1364
Cdd:PRK04863 345 RQQEKIERYQAD--LEELEERL--------EEQNEVVEEADE------QQEENEARAEAAEEEVDELKSQLADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1365 ETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTnyekklaelnfTIQEMKKRSEEDSDIAKELEEsKKKMNKDIETLQR 1444
Cdd:PRK04863 409 QQTRAIQYQQAVQALERAKQLCGLPDLTADNAED-----------WLEEFQAKEQEATEELLSLEQ-KLSVAQAAHSQFE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1445 QIQEL-QAANDRLDKS--KKKIQSELEDATIE--LDTQ----RTKVLELEK---KQKNFDKVLAEEKAISEQVAQERDAA 1512
Cdd:PRK04863 477 QAYQLvRKIAGEVSRSeaWDVARELLRRLREQrhLAEQlqqlRMRLSELEQrlrQQQRAERLLAEFCKRLGKNLDDEDEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1513 EREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELAntqgtadknvhELEKAKRALESQLAELKAQ-NEELED 1591
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA-----------ARAPAWLAAQDALARLREQsGEEFED 625
|
410 420 430
....*....|....*....|....*....|....*...
gi 158285519 1592 DLQLTEDAK--LRLEVNMQALRAQFERDIQAKEEQSEE 1627
Cdd:PRK04863 626 SQDVTEYMQqlLERERELTVERDELAARKQALDEEIER 663
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
1469-1627 |
1.45e-03 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 43.70 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1469 DATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVLSLTRELDEAF-----------EKI 1537
Cdd:PLN03237 1049 DGEIIVNNRKKADLVEELRQKGFTPFPKKAKSVEAAVAGATDDAAEEEEEIDVSSSSGVRGSDYDYllsmaigtltlEKV 1128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1538 DELETKRKGLQNELDELantQGTADKN--VHELEkakrALESQLAELKAQNEELEDDLQLTEDAKLRLE------VNMQA 1609
Cdd:PLN03237 1129 QELCADRDKLNIEVEDL---KKTTPKSlwLKDLD----ALEKELDKLDKEDAKAEEAREKLQRAAARGEsgaakkVSRQA 1201
|
170
....*....|....*...
gi 158285519 1610 LRAQFERDIQAKEEQSEE 1627
Cdd:PLN03237 1202 PKKPAPKKTTKKASESET 1219
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1158-1597 |
1.48e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1158 LAEIQEDL-EAEKLARS----KAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESAnhesTL 1232
Cdd:PRK04778 81 LPDIEEQLfEAEELNDKfrfrKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRK----SL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1233 MDMRHKHAQEISSINEQLENLKKmkgglEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAEtQIAELQVKLADVDRV 1312
Cdd:PRK04778 157 LANRFSFGPALDELEKQLENLEE-----EFSQFVELTESGDYVEAREILDQLEEELAALEQIME-EIPELLKELQTELPD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1313 RV-ELQDKVTKLQQESENITQQLDEAELKAsaaiksagnLESQLTEAQQLLEEetrqkLAL---SSKLRQIESEKEALQE 1388
Cdd:PRK04778 231 QLqELKAGYRELVEEGYHLDHLDIEKEIQD---------LKEQIDENLALLEE-----LDLdeaEEKNEEIQERIDQLYD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1389 QLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIET---LQRQIQELQAANDRLDK---SKKK 1462
Cdd:PRK04778 297 ILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESvrqLEKQLESLEKQYDEITEriaEQEI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1463 IQSELEDatieldtqrtkvlELEKKQKNFDKVLAEEKAISEQVAQERDAaEREAREKETKVLSLTRELDEAFEKI----- 1537
Cdd:PRK04778 377 AYSELQE-------------ELEEILKQLEEIEKEQEKLSEMLQGLRKD-ELEAREKLERYRNKLHEIKRYLEKSnlpgl 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1538 -DELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTE 1597
Cdd:PRK04778 443 pEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1731-1967 |
1.53e-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: 43.21 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1731 TEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTE 1810
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1811 LATEKsnsqnnetlkcglERLNKELKA-KLSEQETALRTKLKAATAASEAKNLNLEKQLENETKERLAVQKANRkleKRI 1889
Cdd:COG4942 99 LEAQK-------------EELAELLRAlYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL---AEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158285519 1890 KELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTlkrKAQRECEDMLESHEALSREVNALKSKLS 1967
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA---ELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1313-1689 |
1.62e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1313 RVELQDKVTKLQQESENITQQLDEAELKASAAiKSAGNLESQLTEAQQLLEEETRQKLALSSK--LRQIESEKEALQEQL 1390
Cdd:pfam09731 74 AVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE-KEATKDAAEAKAQLPKSEQEKEKALEEVLKeaISKAESATAVAKEAK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1391 EEDEEAKTNYEKKLAElnfTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQElQAANDRLDKSKKKiqseLEDA 1470
Cdd:pfam09731 153 DDAIQAVKAHTDSLKE---ASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPET----PPKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1471 TIELDTQRTKVLELEKKQKNFDKvlaeekaISEQVAQERDAAEREAREKETKVLSLTRElDEAFEKiDELETKRKGLQNE 1550
Cdd:pfam09731 225 PEHLDNVEEKVEKAQSLAKLVDQ-------YKELVASERIVFQQELVSIFPDIIPVLKE-DNLLSN-DDLNSLIAHAHRE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1551 LDELAntQGTADKNVHELEKAKRALESQLAELKAQNEELeddlqlTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRR 1630
Cdd:pfam09731 296 IDQLS--KKLAELKKREEKHIERALEKQKEELDKLAEEL------SARLEEVRAADEAQLRLEFEREREEIRESYEEKLR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1631 G------------LVKALRDLEAELDEER---------KQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKqAKKLQ 1689
Cdd:pfam09731 368 TelerqaeaheehLKDVLVEQEIELQREFlqdikekveEERAGRLLKLNELLANLKGLEKATSSHSEVEDENRK-AQQLW 446
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1039-1224 |
1.84e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1039 KKLLEERANDLSQTLAEEEEKAKhLAKLKVKHESTIAELEERLLKDHQQRqeADRSKRKIETEVADLKEQINERRMQIEE 1118
Cdd:pfam15709 322 KALLEKREQEKASRDRLRAERAE-MRRLEVERKRREQEEQRRLQQEQLER--AEKMREELELEQQRRFEEIRLRKQRLEE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1119 MQQQlvKREEELAQTLvridEESAAKAAAQKTQRELESQLAEIQEDLEAEKLARSKAEKQKRdlnEELEALKNELLDSLD 1198
Cdd:pfam15709 399 ERQR--QEEEERKQRL----QLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQ---KELEMQLAEEQKRLM 469
|
170 180
....*....|....*....|....*.
gi 158285519 1199 TTAAQQELRSKREQEVATLKKTLEDE 1224
Cdd:pfam15709 470 EMAEEERLEYQRQKQEAEEKARLEAE 495
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1424-1756 |
1.86e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1424 IAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISE 1503
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1504 QVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELK 1583
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1584 AQNEELEDDLQLTEDAKLRLEVN--MQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLE 1661
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1662 GDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERAR 1741
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*
gi 158285519 1742 RAAEGERDELLEEIN 1756
Cdd:COG4372 324 LAKKLELALAILLAE 338
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1478-1757 |
2.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1478 RTKVLELEKKQKNFDKVLAEEKaiseQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANT 1557
Cdd:COG4372 34 RKALFELDKLQEELEQLREELE----QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1558 QGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRRGLVKALR 1637
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1638 DlEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESE 1717
Cdd:COG4372 190 K-EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 158285519 1718 RKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINS 1757
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1017-1307 |
2.16e-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: 43.02 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1017 KLKKMEEDVALIEDQNHKLvkeKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERL--------------- 1081
Cdd:COG5185 237 GFQDPESELEDLAQTSDKL---EKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIaeytksidikkates 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1082 ----LKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAqTLVRIDEESAAKAAAQKTQRELESQ 1157
Cdd:COG5185 314 leeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKES 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1158 LAEIQEDLE-AEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQE-VATLKKTLEDESANHESTLMDM 1235
Cdd:COG5185 393 LDEIPQNQRgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEI 472
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1236 RHKHAQEISSINEQLENLKK----MKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLA 1307
Cdd:COG5185 473 NRSVRSKKEDLNEELTQIESrvstLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPAS 548
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1443-1774 |
2.67e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1443 QRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRtkvlELEKKQKNFDKVLAEEKAISEQvaQERDAAEREareketk 1522
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRR----KLEEAEKARQAEMDRQAAIYAE--QERMAMERE------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1523 vlsltRELdeafEKIDELETKRKGLQNELDELAntqgtadknvHELEKAkRALESQLAELKAQNEELEDDLQLTEDAKLR 1602
Cdd:pfam17380 348 -----REL----ERIRQEERKRELERIRQEEIA----------MEISRM-RELERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1603 LE----------VNMQALRAQFE----RDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDME 1668
Cdd:pfam17380 408 EEerqrkiqqqkVEMEQIRAEQEearqREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1669 ATLEMNNKVKEDALKQAKklQAQIkdairdaeeakaakeelaaiskESERKVKTLEADLMQLTEDLSSSERARRAAEGER 1748
Cdd:pfam17380 488 RAEEQRRKILEKELEERK--QAMI----------------------EEERKRKLLEKEMEERQKAIYEEERRREAEEERR 543
|
330 340
....*....|....*....|....*..
gi 158285519 1749 DEL-LEEINSNSSKGSLMIDEKRRLEA 1774
Cdd:pfam17380 544 KQQeMEERRRIQEQMRKATEERSRLEA 570
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1005-1205 |
2.68e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1005 QKLQLEKVQLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHL-----AKLKVKHESTIAELEE 1079
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgnEELAREALAEKKSLEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1080 RLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEM--QQQLVKREEELAQTLVRIDEESAAKAAAQKTQRelesq 1157
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkaRLKAAKAQEAVQTSLGSLSTSSATDSFERIEEK----- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158285519 1158 laeiQEDLEAEKLARSKAEkQKRDLNEELEALKNELLDSLDTTAAQQE 1205
Cdd:pfam04012 173 ----IEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1316-1967 |
2.73e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1316 LQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLES-QLTEAQQLLEEETRQKLALSSKLRQIESEKEalqeqleede 1394
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTFWSpELKKERALRKEEAARISVLKEQYRVTQEENQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1395 eaktnyekklaELNFTIQEMKKRSEEDSDIAKELEESKKKMNKD-------IETLQRQIQELQAANDRLDKSKKKIQSEL 1467
Cdd:pfam10174 71 -----------HLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDgedkfstPELTEENFRRLQSEHERQAKELFLLRKTL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1468 EDATIELDTQR----------TKVLE------LEKKQKNFDKVLAEEKAISEQVAQErdaAEREAREKETKVLSLTRELD 1531
Cdd:pfam10174 140 EEMELRIETQKqtlgardesiKKLLEmlqskgLPKKSGEEDWERTRRIAEAEMQLGH---LEVLLDQKEKENIHLREELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1532 EAFEKIDElETKRKGLQNELDELANTQGTADKNVHELE---------------------KAKRALESQLAELKAQNEELE 1590
Cdd:pfam10174 217 RRNQLQPD-PAKTKALQTVIEMKDTKISSLERNIRDLEdevqmlktngllhtedreeeiKQMEVYKSHSKFMKNKIDQLK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1591 DDLQLTEDAKLRLEVNMQALRAQFERDIQ---------AKEEQSEEKRRGLVKALR----DLEAELDEERKQRAAAVAAK 1657
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQhievlkeslTAKEQRAAILQTEVDALRlrleEKESFLNKKTKQLQDLTEEK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1658 KKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEAdlmQLTEDLSSS 1737
Cdd:pfam10174 376 STLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE---ALSEKERII 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1738 ERARRAAEGERDELLEEINSN-------SSKGSLMIDEKRRLEARIAALEEELEEEQSNLELMVDRNRKAQLTIEQLTTE 1810
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLkkenkdlKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1811 LATEKSNSQNNETLKCGlERLNKELKAKLS--EQETAlRTKLKAATAASEAKNL-NLEKQLENETKERlavqkanrklEK 1887
Cdd:pfam10174 533 CSKLENQLKKAHNAEEA-VRTNPEINDRIRllEQEVA-RYKEESGKAQAEVERLlGILREVENEKNDK----------DK 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1888 RIKELTMNIedERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTLKRK-AQRECEDMLESHEALSREVNALKSKL 1966
Cdd:pfam10174 601 KIAELESLT--LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNsQQLQLEELMGALEKTRQELDATKARL 678
|
.
gi 158285519 1967 S 1967
Cdd:pfam10174 679 S 679
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1175-1599 |
2.87e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1175 AEKQKRDLNEELEALKNELLDSLdttAAQQELRSK-----REQEVATLKKTLEDESANHESTLMDM-----RHKHAQEIS 1244
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLL---TAQQQQQQSlnwltRLDELQQEASRRQQALQQALAAEEKAqpqlaALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1245 SINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRV---ELQDKVT 1321
Cdd:PRK10246 291 QLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQwnnELAGWRA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1322 KLQQESEN------ITQQLDEAELKASAAIKSAGNLESQltEAQQLLEEETRQKlALSSKLRQIESEKEALQEQLEEDEE 1395
Cdd:PRK10246 371 QFSQQTSDreqlrqWQQQLTHAEQKLNALPAITLTLTAD--EVAAALAQHAEQR-PLRQRLVALHGQIVPQQKRLAQLQV 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1396 AKTNYEKKLAELNFTIQEMKKRSEEDSD---IAKELEESKKKMnKDIETLQRQIQELQAANDRLDKSKKKIQSEledATI 1472
Cdd:PRK10246 448 AIQNVTQEQTQRNAALNEMRQRYKEKTQqlaDVKTICEQEARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAY---QAL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1473 ELDTQRTKVLELEKKQKNfdkvLAEE--------KAISEQVAQERDAAEREAREKETkvlsLTRELDEAFEKIDELETKR 1544
Cdd:PRK10246 524 EPGVNQSRLDALEKEVKK----LGEEgaalrgqlDALTKQLQRDESEAQSLRQEEQA----LTQQWQAVCASLNITLQPQ 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 1545 KGLQNELDElantQGTADKNVHELEKaKRALESQLAELKAQNEELEDDLQLTEDA 1599
Cdd:PRK10246 596 DDIQPWLDA----QEEHERQLRLLSQ-RHELQGQIAAHNQQIIQYQQQIEQRQQQ 645
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1835-1963 |
3.01e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1835 LKAKLSEQETALRTKLKAATAASEAknlnlEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRhadQYKEQIEKAN 1914
Cdd:pfam02841 178 LQEFLQSKEAVEEAILQTDQALTAK-----EKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQER---SYQEHVKQLI 249
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 158285519 1915 NRMKTLKRNLDEaeeeiQKEKTLKRKAQRECEDMLESH----EALSREVNALK 1963
Cdd:pfam02841 250 EKMEAEREQLLA-----EQERMLEHKLQEQEELLKEGFkteaESLQKEIQDLK 297
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1321-1948 |
3.06e-03 |
|
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: 42.79 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1321 TKLQQESENITQQL--DEAELKASaaiksagnlESQLTEAQQLLEEETR--QKLALSSKLRQIESEKEALQEQLEEDEEA 1396
Cdd:pfam05483 81 SKLYKEAEKIKKWKvsIEAELKQK---------ENKLQENRKIIEAQRKaiQELQFENEKVSLKLEEEIQENKDLIKENN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1397 KTNYEkklaeLNFTIQEMKKRSEEDSDIAKELEESKK---KMNKDIETLQRQIQEL--QAANDRLDKSKKkiqseledat 1471
Cdd:pfam05483 152 ATRHL-----CNLLKETCARSAEKTKKYEYEREETRQvymDLNNNIEKMILAFEELrvQAENARLEMHFK---------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1472 IELDTQRTKVLELEKKQKNFDKvlaeEKAISEQVAQerdaaereAREKETKVLSLTRELDEAFEKIDELETKRKGLQNEL 1551
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDK----EKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1552 DELANTQgtaDKNVHELEKAKRALESQLAELKAQNEELE----DDLQLTEDAKLRLEVNMQALRA--------------- 1612
Cdd:pfam05483 285 KELIEKK---DHLTKELEDIKMSLQRSMSTQKALEEDLQiatkTICQLTEEKEAQMEELNKAKAAhsfvvtefeattcsl 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1613 -QFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKedalKQAKKLQAQ 1691
Cdd:pfam05483 362 eELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFE----KIAEELKGK 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1692 IKDAIrdaeeakaakeelaAISKESERKVKTLEadlMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSlmidekrr 1771
Cdd:pfam05483 438 EQELI--------------FLLQAREKEIHDLE---IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA-------- 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1772 leariaaleeeleeeqsNLELMVDRNRKAQLTIEQLTTELATEKSNSQNNETLKcglERLNKELKaKLSEQETALRTKLK 1851
Cdd:pfam05483 493 -----------------HCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQE---ERMLKQIE-NLEEKEMNLRDELE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1852 AATAASEAKNLNLEKQLENETKERLAVQKANRKLEKRIKELTmniederrhadqykeqiEKANNRMKTLKRNLDEAEEEI 1931
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE-----------------NKCNNLKKQIENKNKNIEELH 614
|
650
....*....|....*..
gi 158285519 1932 QKEKTLKRKAQRECEDM 1948
Cdd:pfam05483 615 QENKALKKKGSAENKQL 631
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1351-1465 |
3.08e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1351 LESQLTE-AQQL-LEEETRQKL-----ALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDsd 1423
Cdd:PRK09039 58 LNSQIAElADLLsLERQGNQDLqdsvaNLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARA-- 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 158285519 1424 iAKELEeskkKMNKDIETLQRQIQELQAAndrLDKSKKKIQS 1465
Cdd:PRK09039 136 -LAQVE----LLNQQIAALRRQLAALEAA---LDASEKRDRE 169
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1268-1368 |
3.09e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1268 EAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKS 1347
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
|
90 100
....*....|....*....|.
gi 158285519 1348 AGnleSQLTEAQQLLEEETRQ 1368
Cdd:PRK11448 221 IT---DQAAKRLELSEEETRI 238
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
945-1355 |
3.18e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 945 EEGRARLVARKQELEELmQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEED 1024
Cdd:pfam19220 6 ELLRVRLGEMADRLEDL-RSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1025 VALIEDQNHKLvkekklleerANDLSQTLAEEEEKAKHLAKLkvkhESTIAELEERLLKDHQQRQEADRSKRKIETEVAD 1104
Cdd:pfam19220 85 LEELVARLAKL----------EAALREAEAAKEELRIELRDK----TAQAEALERQLAAETEQNRALEEENKALREEAQA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1105 LKEQINERRMQIEEMQQQLVKREEELAQTLVRIDEESAAKAAAQKTQRELESQLA-------EIQEDLEAEKLARSKAEK 1177
Cdd:pfam19220 151 AEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDatrarlrALEGQLAAEQAERERAEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1178 QkrdLNEELEALKNElldsldttaaQQELRSKREqevatlkkTLEDESANHESTLMDMRHkhaqEISSINEQLENLKKMK 1257
Cdd:pfam19220 231 Q---LEEAVEAHRAE----------RASLRMKLE--------ALTARAAATEQLLAEARN----QLRDRDEAIRAAERRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1258 GGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQqesENITQQLDEA 1337
Cdd:pfam19220 286 KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLS---DRIAELTKRF 362
|
410
....*....|....*...
gi 158285519 1338 ELKASAAIKSAGNLESQL 1355
Cdd:pfam19220 363 EVERAALEQANRRLKEEL 380
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1343-1925 |
3.18e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1343 AAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNfTIQEMKKRSEED- 1421
Cdd:PRK01156 180 AEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELS-SLEDMKNRYESEi 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1422 ----SDIAKELEESKK---------------------------KMNKDIETLQRQIQELQAANDRLDKSKKKIQ------ 1464
Cdd:PRK01156 259 ktaeSDLSMELEKNNYykeleerhmkiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSvlqkdy 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1465 SELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREketkvlsLTRELDEAFEKIDELETKR 1544
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF-------ISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1545 KGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQ 1624
Cdd:PRK01156 412 NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1625 S---EEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEE 1701
Cdd:PRK01156 492 VkdiDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1702 AKAAKEELAAIS---KESERKVKTLEADLMQLTEDLSSSERARRAAEGERDELLEEINSNSSKGSLMIDEKRRLEariaa 1778
Cdd:PRK01156 572 NALAVISLIDIEtnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE----- 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1779 leeeleeeqsnlelmvdrnrKAQLTIEQLTTELATEKsnsqnnetlkcGLERLNKELKAKLSEQETALRtklkaataase 1858
Cdd:PRK01156 647 --------------------KLRGKIDNYKKQIAEID-----------SIIPDLKEITSRINDIEDNLK----------- 684
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1859 aknlNLEKQLENETKERLAVQKANRKLEKRIKELTMNIEDERRHADQyKEQIEKANNRMKTLKRNLD 1925
Cdd:PRK01156 685 ----KSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES-MKKIKKAIGDLKRLREAFD 746
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1530-1698 |
3.45e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1530 LDEAFEKIDEletkrKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQA 1609
Cdd:COG2433 378 IEEALEELIE-----KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1610 LRAQFERDIQAKEEQSEEKRRglvkaLRDLEAELDEERKQRaaavaakKKLEGDLKDMEatlEMNNKVKEDALKQAKKLQ 1689
Cdd:COG2433 453 ARSEERREIRKDREISRLDRE-----IERLERELEEERERI-------EELKRKLERLK---ELWKLEHSGELVPVKVVE 517
|
....*....
gi 158285519 1690 AQIKDAIRD 1698
Cdd:COG2433 518 KFTKEAIRR 526
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1051-1190 |
3.59e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1051 QTLAE--EEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQL--VKR 1126
Cdd:COG2433 376 LSIEEalEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELseARS 455
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158285519 1127 EEELAqtlVRIDEE-SAAKAAAQKTQRELEsQLAEIQEDLEaEKLARSKaEKQKRDLNEELEALK 1190
Cdd:COG2433 456 EERRE---IRKDREiSRLDREIERLERELE-EERERIEELK-RKLERLK-ELWKLEHSGELVPVK 514
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1831-1958 |
3.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1831 LNKELKAKLSEQETALRTKLKAATAASEA-----------KNLNLEKQLENETKERlavQKANRKLEKRIKELTMNIEDE 1899
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAikkealleakeEIHKLRNEFEKELRER---RNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1900 RRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQkektlkrKAQRECEDMLESHEALSRE 1958
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELE-------ELIEEQLQELERISGLTAE 153
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1529-1646 |
3.63e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1529 ELDEAFEKIDELETKRKGLQNELDELANTQGTADKN-VHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEvnm 1607
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE--- 481
|
90 100 110
....*....|....*....|....*....|....*....
gi 158285519 1608 qalraQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEE 1646
Cdd:COG0542 482 -----QRYGKIPELEKELAELEEELAELAPLLREEVTEE 515
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1260-1385 |
3.89e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1260 LEKSKQQLEAENADLAtelRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVElqdkvtKLQQEsENITQQ-LDEAE 1338
Cdd:COG1566 85 LAQAEAQLAAAEAQLA---RLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQ------ALYKK-GAVSQQeLDEAR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 158285519 1339 LKASAAIKSAGNLESQLTEAQQLLEEETrQKLALSSKLRQIESEKEA 1385
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQ 200
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1083-1435 |
3.91e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.15 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1083 KDHQQRQEADRSK-RKIETEVADLKEQINERRmqieemQQQLVKREEELAQTLvrideesaakaaaQKTQRELESQLAE- 1160
Cdd:PLN03229 418 KVNMKKREAVKTPvRELEGEVEKLKEQILKAK------ESSSKPSELALNEMI-------------EKLKKEIDLEYTEa 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1161 -----IQEDLEAEKLARSKAEKQKRDLN----EELEALKNELLDSLDTTAAQQELRSKRE--QEVATLKKTLEDESANHE 1229
Cdd:PLN03229 479 viamgLQERLENLREEFSKANSQDQLMHpvlmEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEK 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1230 STL-MDMRHKHAQEISSINEQLENLKkmkgglEKSKQQLEAENADLATELRnvnqsrQENDRRRKQAETQIAELqVKLAD 1308
Cdd:PLN03229 559 LKAeINKKFKEVMDRPEIKEKMEALK------AEVASSGASSGDELDDDLK------EKVEKMKKEIELELAGV-LKSMG 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1309 VDRVRV--------------ELQDKVTKLQQE----------SENITQQLDEAELKASAAIKSAGNLESQLTEAqqlLEE 1364
Cdd:PLN03229 626 LEVIGVtkknkdtaeqtpppNLQEKIESLNEEinkkiervirSSDLKSKIELLKLEVAKASKTPDVTEKEKIEA---LEQ 702
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1365 ETRQKLALSSKLRQIESEKEalqeqleedeeaktNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKM 1435
Cdd:PLN03229 703 QIKQKIAEALNSSELKEKFE--------------ELEAELAAARETAAESNGSLKNDDDKEEDSKEDGSRV 759
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
906-1123 |
3.93e-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: 41.67 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 906 LENLSKNSQEYEKKYQQAMEEKTHL---------AEQLQAEIELCAEAEEGRARLVARKQELEELMQDLESRIEEEEERV 976
Cdd:pfam09787 2 LESAKQELADYKQKAARILQSKEKLiaslkegsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 977 NALTSEKKKLQINIQDLEEQLEEEEAARQKLQLEKVQLDAKLKKMEEDvaliedqnhkLVKEKKLLEERANDlsqtLAEE 1056
Cdd:pfam09787 82 AQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEE----------LRRSKATLQSRIKD----REAE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1057 EEKAKHLAKLKVKHESTIAELEERLlkdhQQRQEADRSKrkiETEVADLKEQINERRMQIEEMQQQL 1123
Cdd:pfam09787 148 IEKLRNQLTSKSQSSSSQSELENRL----HQLTETLIQK---QTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
931-1113 |
4.44e-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: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 931 AEQLQAEIELcAEAEEGRARLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEA--ARQKLQ 1008
Cdd:COG1579 3 PEDLRALLDL-QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1009 LEKV----QLDAKLKKMEEDVALIEDQNHKLVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEERLLKD 1084
Cdd:COG1579 82 LGNVrnnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170 180
....*....|....*....|....*....
gi 158285519 1085 HQQRQEAdrsKRKIETEVADLKEQINERR 1113
Cdd:COG1579 162 EAEREEL---AAKIPPELLALYERIRKRK 187
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1426-1748 |
4.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1426 KELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQV 1505
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1506 AQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQ 1585
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1586 NEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEEKRRGLVKALRDLEAELDEERKQRAAAVAAKKKLEGDLK 1665
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1666 DMEATLEMNNKVKEDALKQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAAE 1745
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
...
gi 158285519 1746 GER 1748
Cdd:COG4372 368 ADG 370
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1292-1613 |
4.73e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.05 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1292 RKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKL- 1370
Cdd:pfam09731 143 SATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPp 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1371 ALSSKLRQIESEKEALQEQLEEDEEAKTNYEKklaELNFTIQEMKKRSEEDSDIAKELE-ESKKKMNKDIETLQRqiqEL 1449
Cdd:pfam09731 223 KLPEHLDNVEEKVEKAQSLAKLVDQYKELVAS---ERIVFQQELVSIFPDIIPVLKEDNlLSNDDLNSLIAHAHR---EI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1450 QAANDRLDKSKKKIQSELEDAtieldtqrtkvleLEKKQKNFDKVlaeEKAISEQVAQERDAAEREAR-EKETKVLSLTR 1528
Cdd:pfam09731 297 DQLSKKLAELKKREEKHIERA-------------LEKQKEELDKL---AEELSARLEEVRAADEAQLRlEFEREREEIRE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1529 ELDEAFEKidELETKRKGLQNELDELANTQGT-----ADKNVHE-LEKAKRALESQLAELKAQNEELEddlQLTEDaklR 1602
Cdd:pfam09731 361 SYEEKLRT--ELERQAEAHEEHLKDVLVEQEIelqreFLQDIKEkVEEERAGRLLKLNELLANLKGLE---KATSS---H 432
|
330
....*....|.
gi 158285519 1603 LEVNMQALRAQ 1613
Cdd:pfam09731 433 SEVEDENRKAQ 443
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1478-1650 |
4.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1478 RTKVLELEKKqknFDKVLAEEKAISEQVAQErdaAEREAREKetkVLSLTRELD-EAFEKIDELETKRKGLQNELDELAN 1556
Cdd:PRK12704 30 EAKIKEAEEE---AKRILEEAKKEAEAIKKE---ALLEAKEE---IHKLRNEFEkELRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1557 TQGTADKNVHELEKAKRALESQLAELKAQNEELEddlQLTEDAKLRLEV--NMQALRAQfERDIQAKEEQSEEKRRGLVK 1634
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELE---ELIEEQLQELERisGLTAEEAK-EILLEKVEEEARHEAAVLIK 176
|
170
....*....|....*.
gi 158285519 1635 ALRDlEAELDEERKQR 1650
Cdd:PRK12704 177 EIEE-EAKEEADKKAK 191
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1148-1348 |
5.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1148 QKTQRELESQLAEIQEdlEAEKLARSKAEKQKRDLNEELEALKNELldsldttaaQQELRSKREqEVATLKKTLEDESan 1227
Cdd:PRK12704 30 EAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEF---------EKELRERRN-ELQKLEKRLLQKE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1228 hestlmdmrhkhaqeissineqlENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQ---IAELQV 1304
Cdd:PRK12704 96 -----------------------ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerISGLTA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158285519 1305 KLAD---VDRVRVELQDKVTKLQQESENITQQldEAELKASAAIKSA 1348
Cdd:PRK12704 153 EEAKeilLEKVEEEARHEAAVLIKEIEEEAKE--EADKKAKEILAQA 197
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1371-1486 |
5.49e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1371 ALSSKLRQIESEKEALQEQLEEDEEAK-TNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQEL 1449
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKEL 494
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 158285519 1450 QAANDRLDKSKKKIQSELEDATIE--------------LDTQRTKVLELEK 1486
Cdd:COG0542 495 AELEEELAELAPLLREEVTEEDIAevvsrwtgipvgklLEGEREKLLNLEE 545
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1230-1676 |
5.58e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1230 STLMDMRHKHAQEISSINEQLEnlkkmkgGLEKSKQQLEAENADL---ATELRNVNQSRQENDRRRKQAETQIAELQVKL 1306
Cdd:pfam05622 3 SEAQEEKDELAQRCHELDQQVS-------LLQEEKNSLQQENKKLqerLDQLESGDDSGTPGGKKYLLLQKQLEQLQEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1307 ADVDRVRVELQDKVTklQQESENITQQLDEAELKASAAiksagnlesqltEAQQLLEEETRQKLAlSSKLRQIESEKEAl 1386
Cdd:pfam05622 76 FRLETARDDYRIKCE--ELEKEVLELQHRNEELTSLAE------------EAQALKDEMDILRES-SDKVKKLEATVET- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1387 qeqleedeeaktnYEKKLAELNFTIQEMKKRSEEDSDIAK---ELEESKKKMN---KDIETLQRQIQELQAA-------N 1453
Cdd:pfam05622 140 -------------YKKKLEDLGDLRRQVKLLEERNAEYMQrtlQLEEELKKANalrGQLETYKRQVQELHGKlseeskkA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1454 DRLDKSKKKIQSELEDAT-------IELDTQRTKVLEL------EKKQKNFDKVLAEEKAISEQVAQE------RDAAER 1514
Cdd:pfam05622 207 DKLEFEYKKLEEKLEALQkekerliIERDTLRETNEELrcaqlqQAELSQADALLSPSSDPGDNLAAEimpaeiREKLIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1515 EARE-----------KETKVLSLTRELDEAFEKIDELETKRK-------GLQNELDELANTQGTADKNVHELEKAKRALE 1576
Cdd:pfam05622 287 LQHEnkmlrlgqegsYRERLTELQQLLEDANRRKNELETQNRlanqrilELQQQVEELQKALQEQGSKAEDSSLLKQKLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1577 SQLAELKAQNEELE------DDLQLTEDAKLRLEVN--MQALRAQfERDIQAKEEQSE---EKRRGLVKAL-----RDLE 1640
Cdd:pfam05622 367 EHLEKLHEAQSELQkkkeqiEELEPKQDSNLAQKIDelQEALRKK-DEDMKAMEERYKkyvEKAKSVIKTLdpkqnPASP 445
|
490 500 510
....*....|....*....|....*....|....*.
gi 158285519 1641 AELDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNK 1676
Cdd:pfam05622 446 PEIQALKNQLLEKDKKIEHLERDFEKSKLQREQEEK 481
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1154-1270 |
5.60e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1154 LESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALKNElldsldttaaQQELRSKREQEVATLKKTLEDESANhesTLM 1233
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEE----------EDKLLEEAEKEAQQAIKEAKKEADE---IIK 591
|
90 100 110
....*....|....*....|....*....|....*..
gi 158285519 1234 DMRHKHAQEISSINEQleNLKKMKGGLEKSKQQLEAE 1270
Cdd:PRK00409 592 ELRQLQKGGYASVKAH--ELIEARKRLNKANEKKEKK 626
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1796-1944 |
5.87e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1796 RNRKAQLTIEQLTTELATEKSNSQNNETLKCGLERLNKELKAKLSEQETAL---RTKLKAATAASEAKNLnlEKQLENET 1872
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIkkyEEQLGNVRNNKEYEAL--QKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1873 KERlavqkanRKLEKRIKELTMNIEDERRHADQYKEQIEKANNRMKTLKRNLDEAEEEIQKEKTlKRKAQRE 1944
Cdd:COG1579 103 RRI-------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE-ELEAERE 166
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1541-1744 |
6.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1541 ETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQA 1620
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1621 KEEQSEE-----------------KRRGLVKALRDLEAE-LDEERKQRAAAVAAKKKLEGDLKDMEATLEMNNKVKEDAL 1682
Cdd:COG3883 95 LYRSGGSvsyldvllgsesfsdflDRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158285519 1683 KQAKKLQAQIKDAIRDAEEAKAAKEELAAISKESERKVKTLEADLMQLTEDLSSSERARRAA 1744
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1159-1524 |
6.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1159 AEIQEDLEAEKLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESAnhestlmdmrhk 1238
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1239 haqEISSINEQLENLKKMKGGLEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLAdvdrvrvELQD 1318
Cdd:COG4372 95 ---ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE-------SLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1319 KVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKT 1398
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1399 NYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQR 1478
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 158285519 1479 TKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVL 1524
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
896-1122 |
6.46e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 896 EDELRQIRDKLENLSKNSQEYEKKYQQAMeekthLAEQLQAEIELCAEAEEGRARLVARKQELEELMQDLESRIEEEEER 975
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 976 VNALTSEkkklqiniqdleEQLEEEEAARQKLQLEKVQLDAKLKKMEEDVALIEDQNHKLvkEKKLLEERANDLSQTLAE 1055
Cdd:COG3206 256 LPELLQS------------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL--RAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1056 EEEKAKHLAKLkvkhESTIAELEERLLKDHQQRQEADRSKRKIETEVADLkEQINERRMQIEEMQQQ 1122
Cdd:COG3206 322 LEALQAREASL----QAQLAQLEARLAELPELEAELRRLEREVEVARELY-ESLLQRLEEARLAEAL 383
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
882-1743 |
6.47e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 882 LLEVTKQEEKLVQKEDELRQ----IRDKLeNLSKNSQEYEKK---YQQAMEEkthLAEQLQAEIELCAEAEEGRARLVAR 954
Cdd:COG3096 308 LVEMARELEELSARESDLEQdyqaASDHL-NLVQTALRQQEKierYQEDLEE---LTERLEEQEEVVEEAAEQLAEAEAR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 955 KQELEELMQDLES--------------RIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQlekvQLDAKLKK 1020
Cdd:COG3096 384 LEAAEEEVDSLKSqladyqqaldvqqtRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQ----QATEEVLE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1021 MEEDVALIEDQNHKLVKEKKLLE--------ERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELE---------ERLLK 1083
Cdd:COG3096 460 LEQKLSVADAARRQFEKAYELVCkiageverSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEqrlrqqqnaERLLE 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1084 DHQQRQEADRSKR--------KIETEVADLKEQIN---ERRMQIEEMQQQLVKREEELAQT----------LVRIDEESA 1142
Cdd:COG3096 540 EFCQRIGQQLDAAeeleellaELEAQLEELEEQAAeavEQRSELRQQLEQLRARIKELAARapawlaaqdaLERLREQSG 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1143 AKAaaqKTQRELESQLAEIQEDLEAEKLARSKAEKQKRDLNEELEALknelldSLDTTAAQQELRSKREQEVATLKKTLE 1222
Cdd:COG3096 620 EAL---ADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL------SQPGGAEDPRLLALAERLGGVLLSEIY 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1223 DESANHESTLMDMRH---KHA---QEISSINEQLENLKKMKGGL-----------EKSKQQLEAENADLA-TELRNVNQS 1284
Cdd:COG3096 691 DDVTLEDAPYFSALYgpaRHAivvPDLSAVKEQLAGLEDCPEDLyliegdpdsfdDSVFDAEELEDAVVVkLSDRQWRYS 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1285 RQENDRR--RKQAETQIAELQVKLADVDRVRVELQDKVTKLQ----QESENITQQLD-------EAELKAsaaiksagnL 1351
Cdd:COG3096 771 RFPEVPLfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQrlhqAFSQFVGGHLAvafapdpEAELAA---------L 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1352 ESQLTEAQQLLEEETRQKLALSSKLRQIeseKEALQEQLEEDEEAKTNYEKKLAELnftIQEMkkrsEEDSDIAKELEES 1431
Cdd:COG3096 842 RQRRSELERELAQHRAQEQQLRQQLDQL---KEQLQLLNKLLPQANLLADETLADR---LEEL----REELDAAQEAQAF 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1432 KKKMNKDIETLQRQIQELQ---AANDRLdkskkkiQSELEDATIELDTQRTKVLELEKKQKNF------DKV--LAEEKA 1500
Cdd:COG3096 912 IQQHGKALAQLEPLVAVLQsdpEQFEQL-------QADYLQAKEQQRRLKQQIFALSEVVQRRphfsyeDAVglLGENSD 984
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1501 ISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDEL----ETKRKGLQNELDELANTQGTADKNVHELEKAKRA-L 1575
Cdd:COG3096 985 LNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLkssrDAKQQTLQELEQELEELGVQADAEAEERARIRRDeL 1064
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1576 ESQLAELKAQNEELEDDLQLTEDAklrlevnmqalraqferdiqakeeqseekRRGLVKALRDLEAELDEERKQraaava 1655
Cdd:COG3096 1065 HEELSQNRSRRSQLEKQLTRCEAE-----------------------------MDSLQKRLRKAERDYKQEREQ------ 1109
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1656 akkkLEGDLKDMEATLEM--NNKV------KEDALKQAKKLQAqikdairdaeeakaakeelaaISKESERKVKTLEADL 1727
Cdd:COG3096 1110 ----VVQAKAGWCAVLRLarDNDVerrlhrRELAYLSADELRS---------------------MSDKALGALRLAVADN 1164
|
970
....*....|....*.
gi 158285519 1728 MQLTEDLSSSERARRA 1743
Cdd:COG3096 1165 EHLRDALRLSEDPRRP 1180
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
950-1193 |
6.71e-03 |
|
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: 40.95 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 950 RLVARKQELEELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEEEAARQKLQ----------------LEKVQ 1013
Cdd:pfam15905 84 ALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKakfsedgtqkkmsslsMELMK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1014 LDAKLK-KMEEDVALIEDQNHKLVKEKKLLEERANDLSQTlaeeEEKAKHLAKLKVKHESTIAELEERLLKDHQQRQEAD 1092
Cdd:pfam15905 164 LRNKLEaKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQL----EEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1093 RSKRKIetevADLKEQINERRMQIEEMQQQLVKREEELAqtlvrideesaakaaaqKTQRELESQLAEIQEDLEAEKlar 1172
Cdd:pfam15905 240 KYKLDI----AQLEELLKEKNDEIESLKQSLEEKEQELS-----------------KQIKDLNEKCKLLESEKEELL--- 295
|
250 260
....*....|....*....|.
gi 158285519 1173 SKAEKQKRDLNEELEALKNEL 1193
Cdd:pfam15905 296 REYEEKEQTLNAELEELKEKL 316
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1291-1544 |
6.77e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1291 RRKQAEtQIAELQVkLADVDRVrveLQDKVTKLQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKL 1370
Cdd:PHA02562 152 RRKLVE-DLLDISV-LSEMDKL---NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1371 ALSsklRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKKRSEEDSDIAKELEESKK--KMNKDIETLQRQIQE 1448
Cdd:PHA02562 227 EEA---KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQISEGPDRITK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1449 LQ----AANDRLDKSKKKIQsELEDATIELDTQRTKVLELEKK--QKNFDKVLAEEKAISEQVAQERDAAEREAREKETK 1522
Cdd:PHA02562 304 IKdklkELQHSLEKLDTAID-ELEEIMDEFNEQSKKLLELKNKisTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELA 382
|
250 260
....*....|....*....|..
gi 158285519 1523 vlSLTRELDEAFEKIDELETKR 1544
Cdd:PHA02562 383 --KLQDELDKIVKTKSELVKEK 402
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1260-1627 |
7.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1260 LEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAEL 1339
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1340 KASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKLRQIESEKEALQEQLEEDEEAKTNYEKKLAELNFTIQEMKkrse 1419
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1420 edsdiaKELEESKKKMNKDIETLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEK 1499
Cdd:COG4372 164 ------EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1500 AISEQVAQERDAAEREAREKETKVLSLTRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRALESQL 1579
Cdd:COG4372 238 LLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 158285519 1580 AELKAQNEELEDDLQLTEDAKLRLEVNMQALRAQFERDIQAKEEQSEE 1627
Cdd:COG4372 318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1527-1599 |
7.15e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.21 E-value: 7.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1527 TRELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAK---RALESQLAELKAQNEELEDDLQLTEDA 1599
Cdd:PRK05431 20 KRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAE 95
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
942-1339 |
7.64e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 942 AEAEEGRARLVARKQEL---EELMQDLESRIEEEEERVNALTSEKKKLQINIQDLEEQLEEeeaARQKLqLEK------- 1011
Cdd:PRK04778 91 AEELNDKFRFRKAKHEIneiESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRE---LRKSL-LANrfsfgpa 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1012 -VQLDAKLKKMEED----VALIEDQNHklVKEKKLLEERANDLSQTLAEEEEKAKHLAKLKVKHESTIAELEE---RLLK 1083
Cdd:PRK04778 167 lDELEKQLENLEEEfsqfVELTESGDY--VEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyrELVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1084 DHQQRQEADrskrkIETEVADLKEQINERRMQIEEMqqQLVKREEELAQTLVRIDE-------ESAAKAAAQKTQRELES 1156
Cdd:PRK04778 245 EGYHLDHLD-----IEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQERIDQlydilerEVKARKYVEKNSDTLPD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1157 QLAEIQE---DLEAE--------KLARSKAEKQkRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDES 1225
Cdd:PRK04778 318 FLEHAKEqnkELKEEidrvkqsyTLNESELESV-RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1226 ANHEstlmdmrhKHAQEISSI----NEQLENLKKMKGGLEKSKQQLEAEN-----ADLATELRNVnqsrqenDRRRKQAE 1296
Cdd:PRK04778 397 KEQE--------KLSEMLQGLrkdeLEAREKLERYRNKLHEIKRYLEKSNlpglpEDYLEMFFEV-------SDEIEALA 461
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 158285519 1297 TQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDEAEL 1339
Cdd:PRK04778 462 EELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ 504
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
901-1140 |
7.75e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 901 QIRDKLENLSKNSQEYEKKYQQAMEEKthlAEQLQAEIELCAEAEEGRARLvaRKQELEELMQDLESRIEEEEERVNALT 980
Cdd:PRK05771 32 HIEDLKEELSNERLRKLRSLLTKLSEA---LDKLRSYLPKLNPLREEKKKV--SVKSLEELIKDVEEELEKIEKEIKELE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 981 SEKKKLQINIQDLEEqleeeeaarQKLQLEkvqldaKLKKMEEDVALIEDQNHKLV------KEKKLLEERANDLSQTLA 1054
Cdd:PRK05771 107 EEISELENEIKELEQ---------EIERLE------PWGNFDLDLSLLLGFKYVSVfvgtvpEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1055 EEEEKAKHLAKLKVKHEstIAELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQQQLVKREEELAQTL 1134
Cdd:PRK05771 172 ISTDKGYVYVVVVVLKE--LSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEEL 249
|
....*.
gi 158285519 1135 VRIDEE 1140
Cdd:PRK05771 250 LALYEY 255
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1260-1644 |
7.93e-03 |
|
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: 41.03 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1260 LEKSKQQLEAENADLATELRNVNQSRQENDRRRKQAETQIaelqvkladvDRVRVELQDKVTKLQQESENITQQLDEael 1339
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQW----------ERQRRELESRVAELKEELRQSREKHEE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1340 kasaaiksagnLESQLTEAQQLLEEETRQKLALSsklrqiESEKEALQEQLEEDEEAKTNYEKKLaELNFTIQEMKKRSE 1419
Cdd:pfam07888 99 -----------LEEKYKELSASSEELSEEKDALL------AQRAAHEARIRELEEDIKTLTQRVL-ERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1420 EDSDIAKELEESKKKMNKDIE-------TLQRQIQELQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFd 1492
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQqteeelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1493 KVLAEEKAISEQ-----------VAQERDAAEREAREKETKVLSLTRELDEAFEKIdeletkRKGLQNELDELANTQGTA 1561
Cdd:pfam07888 240 RSLQERLNASERkveglgeelssMAAQRDRTQAELHQARLQAAQLTLQLADASLAL------REGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1562 DKNVHELEKAKRAL---ESQLAELKAQNEELEDDLQLTEDAKL----RLEVNMQALRAQFeRDIQAKEEQSEEKRRGLVK 1634
Cdd:pfam07888 314 EADKDRIEKLSAELqrlEERLQEERMEREKLEVELGREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLE 392
|
410
....*....|
gi 158285519 1635 ALRDLEAELD 1644
Cdd:pfam07888 393 YIRQLEQRLE 402
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1449-1597 |
9.04e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1449 LQAANDRLDKSKKKIQSELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEReAREKETKVLSLTR 1528
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ-AQIDLARRRVLAP 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158285519 1529 ELDEAFEKIDELETKRKGLQNELDELANTQGTADKNVHELEKAKRAL--------ESQLAELKAQNEELEDDLQLTE 1597
Cdd:pfam00529 135 IGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvrselsgaQLQIAEAEAELKLAKLDLERTE 211
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1148-1336 |
9.53e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1148 QKTQRELESQLAEIQEDLEAE-KLARSKAEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQ---EVATLKKtled 1223
Cdd:PHA02562 201 NKNIEEQRKKNGENIARKQNKyDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKiksKIEQFQK---- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1224 esanhestLMDMRHKH------AQEISSINEQLE----NLKKMKGGLEKSKQQLEAENA-------------DLATELRN 1280
Cdd:PHA02562 277 --------VIKMYEKGgvcptcTQQISEGPDRITkikdKLKELQHSLEKLDTAIDELEEimdefneqskkllELKNKIST 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 158285519 1281 VNQSRQENDRRRKQAETQIAELQVKLADVDRVRVELQDKVTKLQQESENITQQLDE 1336
Cdd:PHA02562 349 NKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYH 404
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
1076-1524 |
9.79e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 40.84 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1076 ELEERLLKDHQQRQEADRSKRKIETEVADLKEQINERRMQIEEMQ--QQLVKREEELAQTLVRIdeESAAKAAAQKTQRE 1153
Cdd:COG5644 335 ESERKMHQALLDAGLENESALKKQEELALNKLSVEEVAERTRQLRfmRELMFREERKAKRVAKI--KSKTYRKIRKNRKE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1154 LESQLAEIQEDLEAEK--LARSK---AEKQKRDLNEELEALKNELLDSLDTTAAQQELRSKREQEVATLKKTLEDESANH 1228
Cdd:COG5644 413 KEMALIPKSEDLENEKseEARALermTQRHKNTSSWTRKMLERASHGEGTREAVNEQIRKGDELMQRIHGKEIMDGEDVS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1229 ESTLMDMRHKHAQEISSinEQLENLKKMKGGLekskqqleaenadlatelrnvNQSRQENDRRRKQAETQIAELQ-VKLA 1307
Cdd:COG5644 493 EFSDSDYDTNEQVSTAF--EKIRNEEELKGVL---------------------GMKFMRDASNRQMAASKISVADlVKVE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1308 DVDRVRVELQDKVTklQQESENITQQLDEAELKASAAIKSAGNLESQLTEAQQLLEEETRQKLALSSKlrqieSEKEALQ 1387
Cdd:COG5644 550 NGDDIDVGELDEVG--GDAIYANAGRREVFPVVEQRRKLAPRKRKEDFVTPSTSLEKSMDRILHGQKK-----RAEGAVV 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158285519 1388 EQLEEDEEAKTNYEkkLAELNFTIQEMKKRSEEDSDIAKELEESKKKMNKDIETL--QRQIQELQAANDRLDKSKKKIQS 1465
Cdd:COG5644 623 FEKPLEATENFNPW--LDRKMRRIKRIKKKAYRRIRRDKRLKKKMPEEENTQENHlgSEKKRHGGVPDILLKEIEVEDDE 700
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 158285519 1466 ELEDATIELDTQRTKVLELEKKQKNFDKVLAEEKAISEQVAQERDAAEREAREKETKVL 1524
Cdd:COG5644 701 KTPILSPGGDEEVEEGLSIKTQEELVALAFAGDDVVAEFEEEKREIVNREAPKEEDVVL 759
|
|
| |
